@article{Abdeldaiem2019,
author = {Abdeldaiem, A. M and El-bagoury, Ekram H and Abbas, Fka and Faisal, M A},
doi = {10.21608/ijds.2019.58500},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/IJDS_Volume 6_Issue 1_Pages 1-7.pdf:pdf},
journal = {Ismailia Journal of Dairy Science & Technology},
keywords = {bromelain,cichorium,crude-plant-enzymes extracts,papain,proteolytic activities},
number = {1},
pages = {1--7},
title = {{Effect of some Factors on the Proteolytic Activities of Bromelain, Cichorium and Papain Extracts}},
volume = {6},
year = {2019}
}
@article{Agrahari2014,
abstract = {Natural senescence is associated with several fold increase in activity of protease and is characterized by the degradation and loss of proteins therefore plant proteases have been a common studied interestingly. Protease from senesced leaves of the papaya plant (Carica Papaya) was partially purified by ammonium sulfate precipitation. It showed 15 fold purification. Optimum protease activity was found at alkaline range 9 and 60°C. Mn 2+ ion had the least effect on the activity of the enzyme. While Cu 2+ showed the maximum inhibitory effect on the protease activity. The enzyme was then used in further application in the detergent industry. We reported that the enzyme remained active and can be used to destain protein stains (blood, leaf extract, flower pigment and turmeric) from prestained cloth. The easy availability of the senesced leaves of this common plant makes it a cheaper enzyme source and potential additive in detergents.},
author = {Agrahari, Sarita and Sharma, Neha},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/ijgebv5n1_04.pdf:pdf},
journal = {International Journal of Genetic Engineering and Biotechnology},
keywords = {Casein,Protease,Purification,Senesced leaves,papaya},
number = {1},
pages = {29--34},
title = {{Extraction and Characterization of Protease From Senesced Leaves of Papaya (Carica Papaya) and It's Application}},
url = {http://www.irphouse.com},
volume = {5},
year = {2014}
}
@article{Amri2012,
abstract = {Papain is a plant proteolytic enzyme for the cysteine proteinase family cysteine protease enzyme in which enormous progress has been made to understand its functions. Papain is found naturally in papaya (Carica papaya L.) manufactured from the latex of raw papaya fruits. The enzyme is able to break down organic molecules made of amino acids, known as polypeptides and thus plays a crucial role in diverse biological processes in physiological and pathological states, drug designs, industrial uses such as meat tenderizers and pharmaceutical preparations. The unique structure of papain gives it the functionality that helps elucidate how proteolytic enzymes work and also makes it valuable for a variety of purposes. In the present review, its biological importance, properties and structural features that are important to an understanding of their biological function are presented. Its potential for production and market opportunities are also discussed. {\textcopyright} 2012 Science Publication.},
author = {Amri, Ezekiel and Mamboya, Florence},
doi = {10.3844/ajbbsp.2012.99.104},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/ajbbsp.2012.99.104-with-cover-page.pdf:pdf},
issn = {15533468},
journal = {American Journal of Biochemistry and Biotechnology},
keywords = {Cysteine protease,Hydrophobic,Papain,Proteolytic enzyme,Structure},
number = {2},
pages = {99--104},
title = {{Papain, a plant enzyme of biological importance: A review}},
volume = {8},
year = {2012}
}
@book{Barekat2017,
abstract = {The present study aims to develop a novel process for improving meat tenderness. Three muscles were selected among five young Holstein bulls Longissimus lumborum muscles and were cut into 3 × 3 × 3 cm pieces. Samples were sonicated by ultrasonic probe (20 kHz) at power of 100 and 300 W for 10, 20, and 30 min both in the presence and absence of 0.1% papain enzyme solution. The effects of treatments were investigated on proteolytic activity, filtering residues, Warner–Bratzler shear force (WBSF), meat textural profile (TPA), and muscle microstructure. Application of enzyme, either singly or coupled with ultrasound significantly (P < 0.05) decreased the filtering residue, WBSF and textural parameters. The most proteolytic activity and the highest tenderness were obtained when the combined treatment was applied at ultrasonic power of 100 W for 20 min. Finally, the results showed that, combined treatment can be employed as a useful tool for the meat tenderization.},
author = {Barekat, Sorour and Soltanizadeh, Nafiseh},
booktitle = {Innovative Food Science and Emerging Technologies},
doi = {10.1016/j.ifset.2016.12.009},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/j.ifset.2016.12.009.pdf:pdf},
isbn = {8415683111},
issn = {14668564},
keywords = {Enzyme activity,Longissimus lumborum,Papain,Tenderness,Ultrasound},
pages = {223--229},
publisher = {Elsevier Ltd},
title = {{Improvement of meat tenderness by simultaneous application of high-intensity ultrasonic radiation and papain treatment}},
url = {http://dx.doi.org/10.1016/j.ifset.2016.12.009},
volume = {39},
year = {2017}
}
@article{Bhat2018,
abstract = {The tenderization process, which can be influenced by both pre- and post-slaughter interventions, begins immediately after an animal's death and is followed with the disruption of the muscle structure by endogenous proteolytic systems. The post-slaughter technological interventions like electrical stimulation, suspension methods, blade tenderization, tumbling, use of exogenous enzymes, and traditional aging are some of the methods currently employed by the meat industry for improving tenderness. Over the time, technological advancement resulted in development of several novel methods, for maximizing the tenderness, which are being projected as quick, economical, nonthermal, green, and energy-efficient technologies. Comparison of these advanced technological methods with the current applied industrial methods is necessary to understand the feasibility and benefits of the novel technology. This review discusses the benefits and advantages of different emerging tenderization techniques such as hydrodynamic-pressure processing, high-pressure processing, pulsed electric field, ultrasound, SmartStretch™, Pi-Vac Elasto-Pack{\textregistered} system, and some of the current applied methods used in the meat industry.},
author = {Bhat, Zuhaib F. and Morton, James D. and Mason, Susan L. and Bekhit, Alaa El Din A.},
doi = {10.1111/1541-4337.12356},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/1541-4337.12356.pdf:pdf},
issn = {15414337},
journal = {Comprehensive Reviews in Food Science and Food Safety},
keywords = {conventional methods,high-pressure processing hydrodynamic-pressure pro,meat tenderization,pulsed electric field,ultrasound},
number = {4},
pages = {841--859},
title = {{Applied and Emerging Methods for Meat Tenderization: A Comparative Perspective}},
volume = {17},
year = {2018}
}
@article{Budama-Kilinc2018,
abstract = {Papain is a protease enzyme with therapeutic properties that are very valuable for medical applications. Poly($\epsilon$-caprolactone) (PCL) is an ideal polymeric carrier for controlled drug delivery systems due to its low biodegradability and its high biocompatibility. In this study, the three-dimensional structure and action mechanism of papain were investigated by in vitro and in silico experiments using molecular dynamics (MD) and molecular docking methods to elucidate biological functions. The results showed that the size of papain-loaded PCL nanoparticles (NPs) and the polydispersity index (PDI) of the NPs were 242.9 nm and 0.074, respectively. The encapsulation efficiency and loading efficiency were 80.4 and 27.2%, respectively. Human embryonic kidney cells (HEK-293) were used for determining the cytotoxicity of papain-loaded PCL and PCL nanoparticles. The in vitro cell culture showed that nanoparticles are not toxic at low concentrations, while toxicity slightly increases at high concentrations. In silico studies, which were carried out with MD simulations and ADME analysis showed that the strong hydrogen bonds between the ligand and the papain provide stability and indicate the regions in which the interactions occur.},
author = {Budama-Kilinc, Yasemin and Cakir-Koc, Rabia and Kecel-Gunduz, Serda and Zorlu, Tolga and Kokcu, Yagmur and Bicak, Bilge and Karavelioglu, Zeynep and Ozel, Aysen E.},
doi = {10.1007/s10895-018-2276-6},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/Budama-Kilinc2018_Article_PapainLoadedPolyΕ-Caprolactone.pdf:pdf},
issn = {10530509},
journal = {Journal of Fluorescence},
keywords = {Enzyme,Fluorescence,HEK-293,Imaging,Molecular docking,Molecular dynamic,PCL,Papain},
number = {5},
pages = {1127--1142},
pmid = {30097974},
publisher = {Journal of Fluorescence},
title = {{Papain Loaded Poly($\epsilon$-Caprolactone) Nanoparticles: In-silico and In-Vitro Studies}},
volume = {28},
year = {2018}
}
@article{Calkins2001,
abstract = {Importance of Beef Tenderness Beef palatability is affected by many factors and tenderness is cited as one of the most important. Consumers are willing to pay a premium for a guaranteed tender product with the potential to increase the value of the middle meats over $60 per carcass (Miller et al., 2001). Consequently, the meat industry is in a continual search for methods to improve the tenderness of the middle meats and upgrade other cuts and muscles to steak quality. This search for tender product not only adds value to the industry but can help to supply a more consistent and uniform product to consumers while increasing overall beef satisfaction. Tenderness is a complex trait. Generally, the two primary structural features of muscle that influence tenderness are integrity of the myofibrils (termed the actomyosin effect) and the connective tissue contribution (termed a background effect). Fat also plays a minor role. Cover et al. (1962) identified six characteristics of perceived tenderness. Three characteristics relate to the myofibrillar portion, two relate to product adhesion, and the remaining one relates to connective tissue components. Myofibrillar proteins are located intracellularly while connective tissue proteins (primarily collagen) are located extracellularly. This difference in distribution of key proteins within the muscle increases the challenge of improving tenderness. Stated simply, some muscles may lack palatability because of myofibrillar proteins while others may lack palatability because of the connective tissue proteins. A plausible tenderization strategy should target one or both of the main structural constraints to be successful.},
author = {Calkins, Chris R and Sullivan, Gary},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/10.1.1.513.5054.pdf:pdf},
title = {{Adding Enzymes to Improve Beef Tenderness Inherent Proteolytic Enzymes}},
url = {www.beefresearch.org},
year = {2001}
}
@article{DellaMalva2017,
abstract = {The aim of this study was to evaluate the effect of dietary supplementation of linseed and/or quinoa on tenderness and on proteome of lamb meat. Thirty-two Italian Merino lambs were distributed into 4 groups with different diet: control (CO) with no supplemental fat, linseed (LS), quinoa (QS) and QS + LS diets. Meat obtained by lamb fed linseed showed the lowest values of WBSF (P < 0.001), hardness (P < 0.01), gumminess (P < 0.01) and chewiness (P < 0.01). Proteomic changes of myofibrillar and sarcoplasmic proteins were estimated with SDS-PAGE, Western Blot and Two-Dimensional Gel Electrophoresis. In linseed group proteomic analysis revealed a degradation of desmin and TnT proteins complex and a major number of spots and phosphorylation isoforms of fast MLC2 patterns. Meat obtained by lamb fed quinoa showed a minor effect on the instrumental evaluation of meat tenderness and a major number of spots ascribed to sarcoplasmic proteins and fMHC. Data suggest that dietary supplementation may act on meat tenderness and on proteolytic pattern of myofibrillar fraction.},
author = {della Malva, Antonella and Marino, Rosaria and Santillo, Antonella and Annicchiarico, Giovanni and Caroprese, Mariangela and Sevi, Agostino and Albenzio, Marzia},
doi = {10.1016/j.meatsci.2017.04.235},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/j.meatsci.2017.04.235.pdf:pdf},
issn = {03091740},
journal = {Meat Science},
keywords = {Lamb meat,Linseed,Myosin light chain 2,Quinoa,Tenderness,Troponin T},
pages = {74--81},
pmid = {28482234},
publisher = {Elsevier Ltd},
title = {{Proteomic approach to investigate the impact of different dietary supplementation on lamb meat tenderness}},
url = {http://dx.doi.org/10.1016/j.meatsci.2017.04.235},
volume = {131},
year = {2017}
}
@article{Denessiouk2020,
abstract = {There are several families of cysteine proteinases with different folds – for example the (chymo)trypsin fold family and papain-like fold family – but in both families the hydrolase activity of cysteine proteinases requires a cysteine residue as the catalytic nucleophile. In this work, we have analyzed the topology of the active site regions in 146 three-dimensional structures of proteins belonging to the Papain-like Cysteine Proteinase (PCP) superfamily, which includes papain as a typical representative of this protein superfamily. All analyzed enzymes contain a unique structurally closed conformation – a “PCP-Zone” – which can be divided into two groups, Class A and Class B. Eight structurally conserved amino acids of the PCP-Zone form a common Structural Core. The Structural Core, catalytic nucleophile, catalytic base and residue Xaa – which stabilizes the side-chain conformation of the catalytic base – make up a PCP Structural Catalytic Core (PCP-SCC). The PCP-SCC of Class A and Class B are divided into 5 and 2 types, respectively. Seven variants of the mutual arrangement of the amino-acid side chains of the catalytic triad – nucleophile, base and residue Xaa – within the same fold clearly demonstrate how enzymes with the papain-like fold adapt to the need to perform diverse functions in spite of their limited structural diversity. The roles of both the PCP-Zone of SARS-CoV-2-PLpro described in this study and the NBCZone of SARS-CoV-2-3CLpro presented in our earlier article (Denesyuk AI, Johnson MS, Salo-Ahen OMH, Uversky VN, Denessiouk K. Int J Biol Macromol. 2020;153:399-411) that are in contacts with inhibitors are discussed.},
author = {Denessiouk, Konstantin and Uversky, Vladimir N. and Permyakov, Sergei E. and Permyakov, Eugene A. and Johnson, Mark S. and Denesyuk, Alexander I.},
doi = {10.1016/j.ijbiomac.2020.10.022},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/denessiouk2020.pdf:pdf},
issn = {18790003},
journal = {International Journal of Biological Macromolecules},
keywords = {COVID-19,Catalytic triad,Cysteine proteinases,Fold,Papain,SARC-CoV-2,Structural catalytic core,Zone},
pages = {1438--1446},
pmid = {33058970},
publisher = {Elsevier B.V.},
title = {{Papain-like cysteine proteinase zone (PCP-zone) and PCP structural catalytic core (PCP-SCC) of enzymes with cysteine proteinase fold}},
url = {https://doi.org/10.1016/j.ijbiomac.2020.10.022},
volume = {165},
year = {2020}
}
@article{Ertbjerg2017,
abstract = {The basic contractile unit of muscle, the sarcomere, will contract as the muscle goes into rigor post-mortem. Depending on the conditions, such as the rate of pH decline, the cooling rate and the mechanical restraints on the muscles, this longitudinal shortening will result in various post-mortem sarcomere lengths as well as lateral differences in the distances between the myosin and actin filaments. This shortening is underlying the phenomena described as rigor contraction, thaw rigor, cold shortening and heat shortening. The shortening in combination with the molecular architecture of the sarcomere as defined by the myosin filaments and their S-1 and S-2 units, the interaction with the actin filaments, and the boundaries formed by the Z-disks will subsequently influence basic meat quality traits including tenderness and water-holding capacity. Biochemical reactions from proteolysis and glycogen metabolism interrelate with the sarcomere length in a complex manner. The sarcomere length is also influencing the eating quality of cooked meat and the water-holding in meat products.},
author = {Ertbjerg, Per and Puolanne, Eero},
doi = {10.1016/j.meatsci.2017.04.261},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/j.meatsci.2017.04.261.pdf:pdf},
issn = {03091740},
journal = {Meat Science},
keywords = {Cold shortening,Heat shortening,Rigor contraction,Tenderness,Thaw rigor,Water-holding},
pages = {139--152},
pmid = {28552497},
publisher = {Elsevier Ltd},
title = {{Muscle structure, sarcomere length and influences on meat quality: A review}},
url = {http://dx.doi.org/10.1016/j.meatsci.2017.04.261},
volume = {132},
year = {2017}
}
@article{Fernandez-Lucas2017,
abstract = {Background In recent years, proteases have arisen as standard biocatalysts in many industrial processes in different fields, such as pharmaceutical, medicine, detergent manufacturing and food science. Among them, papain is undoubtedly one of the most frequently studied and widely used proteases in the food industry around the world. However, the latest advances in recombinant papain expression systems, genetically engineered biocatalysts, new purification and isolation strategies, and enzymatic immobilization will enhance the development of new applications of papain, as well as improve and optimize classical applications. Scope and approach This review addresses not only the latest advances in classic applications, such as meat tenderization and protein hydrolysates, but also the most innovative applications in different industries such as food, animal feed, bioactive peptides production, water treatment, baking and brewing, among many others. In addition, papain is a perfect example of a successful industrial enzyme that covers all the steps of the biocatalytic cycle that are necessary for the industrial implementation of any biocatalyst. This cycle includes the production and extraction of the enzyme concerned (from natural or recombinant sources), functional and structural characterization, genetic improvement, immobilization and, finally, industrial application. This review describes the complete biocatalytic cycle of papain. Key findings and conclusions Papain is clearly a case of industrial and commercial success over the last 40 years. The key to this success has been continual biotechnological and process engineering innovation, which has opened up a new range of possibilities for this exciting biocatalyst. However, further efforts are needed in protein engineering and characterization of new mutants to reach the full potential of this enzyme.},
author = {Fern{\'{a}}ndez-Lucas, Jes{\'{u}}s and Casta{\~{n}}eda, Daniel and Hormigo, Daniel},
doi = {10.1016/j.tifs.2017.08.017},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/1-s2.0-S0924224417301838-main.pdf:pdf;:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/j.tifs.2017.08.017.pdf:pdf},
issn = {09242244},
journal = {Trends in Food Science and Technology},
keywords = {,Biocatalysis,Cysteine proteases,Enzyme biotechnology,Immobilization,Industrial processes,Papain},
number = {2017},
pages = {91--101},
publisher = {Elsevier Ltd},
title = {{New trends for a classical enzyme: Papain, a biotechnological success story in the food industry}},
url = {http://dx.doi.org/10.1016/j.tifs.2017.08.017},
volume = {68},
year = {2017}
}
@article{Gao2017,
abstract = {The objective of this study was to investigate the relationship between the dephosphorylation of myosin regulatory light chain and actin–myosin interaction after muscle homogenate was treated with alkaline phosphatase and phosphatase inhibitor. The myosin regulatory light chain was significantly dephosphorylated by alkaline phosphatase after incubation. Among different groups, dephosphorylated myosin regulatory light chain to a much greater extent leads to a lower actomyosin dissociation degree, thereby raising the actomyosin ATPase activity, whereas it exhibits a higher actomyosin dissociation degree and a lower actomyosin ATPase activity when the myosin regulatory light chain was in a low dephosphorylated state. The data suggest that the dephosphorylation of myosin regulatory light chain modulates actomyosin dissociation (the number of myosin interact with actin) negatively and has a positive influence on actomyosin ATPase activity (the interacting force between myosin and actin).},
author = {Gao, Xing and Li, Xin and Li, Zheng and Du, Manting and Zhang, Dequan},
doi = {10.1111/ijfs.13343},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/ijfs.13343.pdf:pdf},
issn = {13652621},
journal = {International Journal of Food Science and Technology},
keywords = {ATPase activity,Actomyosin dissociation,dephosphorylation,myosin regulation light chain},
number = {6},
pages = {1400--1407},
title = {{Dephosphorylation of myosin regulatory light chain modulates actin–myosin interaction adverse to meat tenderness}},
volume = {52},
year = {2017}
}
@article{Gerelt2000,
abstract = {The treatment of proteolytic enzymes is one of the popular methods for meat tenderization. In this case, it is very important how to introduce the enzymes into the meat cut. This paper describes meat tenderization by dipping the meat cut in a solution containing proteolytic enzymes after contact-osmotic dehydration. After the dehydration of each piece of meat from culled cow for 18 h by contact-dehydration sheet, each sample was dipped for 3 h in a solution containing papain or proteinases from Aspergillus traditionally used for soysauce production in Japan. It was stored at 3$\sim$4°C for 24, 48 and 168 h, and subjected to texture measurement, sensory evaluations, biochemical analysis and histological observations. The penetration efficiency of the enzyme solution (of around 80%) after the contact-osmotic dehydration seemed to be sufficient. A marked decrease in hardness by texture measurements was observed in the meats treated with proteolytic enzymes and higher sensory scores for tenderness were observed in the meats treated with enzymes as compared with the untreated meat. The papain-treated meat received the highest score in tenderness, but the scores given to juiciness and taste were lower than that of the control. The rapid increases of the fragmentation of myofibrils from the enzyme-treated meat were observed at first 24 h of storage as compared with that of the control. Remarkable degradation of myosin molecule in the myofibrils from the enzyme-treated meats was observed on SDS-PAGE profiles. Considerable degradation of myofibrilar structure especially due to proteolytic removal of Z-lines, was observed among the myofibrils from enzyme-treated meats by electronmicroscopy. The remarkable deformation and disruption of honeycomb-like structure of endomysium were also observed in the meats treated with enzymes. From these results, it was shown that treatment after osmotic dehydration, was effective in tenderizing. {\textcopyright} 2000 Elsevier Science Ltd.},
author = {Gerelt, B. and Ikeuchi, Y. and Suzuki, A.},
doi = {10.1016/S0309-1740(00)00060-7},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/s0309-1740%2800%2900060-7.pdf:pdf},
issn = {03091740},
journal = {Meat Science},
keywords = {Intramuscular connective tissue,Meat tenderization,Myofibrils,Osmotic dehydration,Proteolytic enzymes},
number = {3},
pages = {311--318},
title = {{Meat tenderization by proteolytic enzymes after osmotic dehydration}},
volume = {56},
year = {2000}
}
@article{Hafid2020,
abstract = {Three Phase Partitioning (TPP) system as an elegant non-chromatographic and bulk separation method was successfully applied for the extraction and recovery of papain from the latex of Carica papaya. The optimized parameters of TPP allowed achieving a purification fold of 11.45 and activity recovery of 134% with 40% (NH4)2SO4, 1.0:0.75 ratio of crude extract: t-BuOH at pH and temperature of 6.0 and 25 °C, respectively. The recovered papain had a molecular weight of 23.2 kDa and revealed maximum activity at pH 6.0 and temperature of 50 °C. The maximum values of Km and Vmax parameters were 10.83 mg mL−1 and 33.33 U mL−1, respectively. The protease with 4 isoforms was stable at 40–80 °C and a pH range of 6.0–7.5 against numerous metal ions and none of them inactivated the recovered protease. Moreover, 10 mM Ca2+ improved 2-folds the activity and half-life of the protease at temperatures from 30 to 50 °C. The milk-clotting activity tests revealed high stability of latex papain at storage, namely at −20 °C compared to 4 °C and 25 °C for up than 5 weeks. As a meat tenderizing agent, it showed promising role under different treatments by improving the texture of tough meat. The findings indicated that one-step TPP system is a simple, quick, economical and very attractive process for fast recovery of latex papain compared to other proposed protocols.},
author = {Hafid, Kahina and John, James and Sayah, Taha Mansour and Dom{\'{i}}nguez, Rub{\'{e}}n and Becila, Samira and Lamri, Melisa and Dib, Amira Leila and Lorenzo, Jos{\'{e}} M. and Gagaoua, Mohammed},
doi = {10.1016/j.ijbiomac.2019.10.048},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/j.ijbiomac.2019.10.048.pdf:pdf},
issn = {18790003},
journal = {International Journal of Biological Macromolecules},
keywords = {Enzyme activity,Papain,Plant proteases,Separation,Three phase partitioning},
pages = {798--810},
pmid = {31726142},
publisher = {Elsevier LTD},
title = {{One-step recovery of latex papain from Carica papaya using three phase partitioning and its use as milk-clotting and meat-tenderizing agent}},
url = {https://doi.org/10.1016/j.ijbiomac.2019.10.048},
volume = {146},
year = {2020}
}
@article{Holyavka2019,
abstract = {Our research has shown that the degree of photosensitivity of the cysteine proteases can be arranged in the following order: bromelain → ficin → papain. After the UV irradiation with 151 J{\textperiodcentered}m−2 intensity of a bromelain solution, the enzyme activity has increased. No decrease in the catalytic capacity and the change in the size of the molecule was recorded in the 151–6040 J{\textperiodcentered}m−2 range of irradiation intensities. A decrease in the catalytic capacity of ficin and the increase of its globule size occurred after exposure to a radiation of 3020 J{\textperiodcentered}m−2 intensity. The decrease in papain activity was observed at the UV irradiation intensity of 453 J{\textperiodcentered}m−2, and an increase of the papain globule size was detected at 755 J{\textperiodcentered}m−2. Immobilization on chitosan matrix leads to the increase in the stability of heterogeneous biocatalysts with respect to UV irradiation in comparison with free enzymes. The changes in IR spectra of immobilized cysteine proteases practically do not affect the bands due to the protein component of the system: amide I, amide II, amide III. Therefore, it can be postulated that the chitosan matrix acts as photoprotector for immobilized ficin, bromelain and papain. The obtained results can be helpful for development of drugs based on chitosan and cysteine proteases in combination with phototherapy, as well as for choosing their sterilization conditions.},
author = {Holyavka, Marina and Pankova, Svetlana and Koroleva, Victoria and Vyshkvorkina, Yuliya and Lukin, Anatoliy and Kondratyev, Maxim and Artyukhov, Valeriy},
doi = {10.1016/j.jphotobiol.2019.111681},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/j.jphotobiol.2019.111681.pdf:pdf},
issn = {18732682},
journal = {Journal of Photochemistry and Photobiology B: Biology},
keywords = {Adsorption immobilization,Bromelain,Chitosan,Ficin,Papain,UV irradiation},
number = {October},
pages = {111681},
pmid = {31704638},
publisher = {Elsevier},
title = {{Influence of UV radiation on molecular structure and catalytic activity of free and immobilized bromelain, ficin and papain}},
url = {https://doi.org/10.1016/j.jphotobiol.2019.111681},
volume = {201},
year = {2019}
}
@article{Hu2018,
abstract = {This study was conducted to assess the potential application of ultrasonic treatment to enhance the tenderness of whelk (Buccinum undatum) meat. The optimum ultrasonic conditions for the maximum tenderization effect were determined using response surface methodology by a three-level factorial Box–Behnken design for the optimization of three variables. The optimum conditions for the three variables found were as follows: ultrasound power at 200 W, treatment time for 9.6 min, and temperature at 45°C. The resulted tenderization effect was comparable to traditional enzymatic methods. Furthermore, disruption of muscle microstructure was observed in the ultrasonic-treated whelk meat by scanning electron microscopy, while evaluations on physicochemical properties indicated the ultrasonic treatment has no significant undesirable effects on the quality of whelk meat including pH, water-holding capacity, and lipid oxidation. In conclusion, this study showed the feasibility of ultrasonic treatment as a promising tenderization method for whelk meat without detrimental effects on its quality.},
author = {Hu, Jiamiao and Ge, Shenghan and Huang, Chenying and Cheung, Peter C.K. and Lin, Luan and Zhang, Yi and Zheng, Baodong and Lin, Shaoling and Huang, Xiujuan},
doi = {10.1002/fsn3.686},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/fsn3.686.pdf:pdf},
issn = {20487177},
journal = {Food Science and Nutrition},
keywords = {Buccinum undatum,response surface methodology,tenderization,ultrasound},
number = {7},
pages = {1848--1857},
title = {{Tenderization effect of whelk meat using ultrasonic treatment}},
volume = {6},
year = {2018}
}
@article{Ikram2021,
author = {Ikram, Ali and Ambreen, Saadia and Azhar, Areeg and Khalid, Waseem},
doi = {10.12692/ijb/18.1.102-112},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/IJB-Vol-18-No-1-p-110-112.pdf:pdf},
journal = {International Journal of Biosciences},
keywords = {1,10,102-112,12692,18,bromelain,doi,dx,ficin,http,ijb,meat tenderization,org,papain,proteases},
number = {1},
pages = {102--112},
title = {{Meat Tenderization through Plant Proteases-A Mini Review}},
volume = {18},
year = {2021}
}
@article{Istrati2008,
abstract = {From all types of treatments used to improve meat tenderness (mechanical, chemical, enzymatic tenderization), has been studied the enzymatic tenderization with papain a tropical plant enzyme derived from papaya. In this research has been evaluated papain influence on adult beef because pork, mutton and chicken meat are enough tender. Papain was added in injection brine and than the beef cuts was injected with a specific percent of brine. Experimental data indicate that papain weaken beef meat structure produced improvement of functional properties of adult beef. Papain attacks connective tissue and myofibril proteins determinate increase of hydroxiproline and free amino acids content in boiled beef cuts. A significant increase in tenderness by rigidity index measurement was observed in the meats treated with papain as compared with the control. The sensorial tests of beef treated with papain were bigger than control. This experiment confirms that papain is a proteolytic enzyme that causes improvement of meat quality.},
author = {Istrati, Daniela},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/The_influence_of_enzymatic_tenderization_with_papa.pdf:pdf},
journal = {Journal of Agroalimentary Processes and Technologies},
keywords = {Tenderness,adult beef,papain,rigidity index ___________________________________},
number = {January 2008},
pages = {140--146},
title = {{The influence of enzymatic tenderization with papain on functional properties of adult beef}},
url = {www.tpa-timisoara.ro},
volume = {14},
year = {2008}
}
@article{Jun-hui2020,
abstract = {Jumbo squid (Dosidicus gigas) muscle is rather hard and tough, which directly affects consumer acceptance. In this study, the tenderization effect of bromelain and papain on squid muscle during enzymolysis is examined and compared with an untreated control and water-treated sample. Squid mantle were incubated with different solutions (water, bromelain, and papain solution) for 40 min in a 30 °C water bath. Then, the mantle samples were subjected to water holding capacity (WHC) analysis, texture evaluation, biochemical determination, and histological observations. The results revealed that bromelain and papain disadvantageously decrease the water holding capacity when compared to the control and water-treated samples. Furthermore, following tenderization with bromelain or papain, muscle hardness, shear force, myofibrillar protein content, and Ca2+ ATPase activity were all significantly decreased. Additionally, some essential amino acids were released following tenderization. When examining the myofibrillar fragmentation index (MFI), bromelain and papain were shown to cause high levels of hydrolysis in myofibrillar and sarcoplasmic proteins. Moreover, microstructural imaging indicated that the tenderization treatments disrupted myofibrils and generated a larger number of small fragments in the muscle tissues, subsequently decreasing microstructure stability and integrity. SDS-PAGE analysis confirmed that bromelain and papain have a high proteolytic activity, with some small peptides and/or short fragments detected post-tenderization. The results presented herein demonstrated that bromelain and papain improved squid muscle tenderness and can be utilized to ensure a more desirable squid product.},
author = {Jun-hui, Xu and Hui-juan, Cao and Bin, Zhang and Hui, Yao},
doi = {10.1016/j.foodres.2020.108991},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/j.foodres.2020.108991.pdf:pdf},
issn = {18737145},
journal = {Food Research International},
keywords = {Acetic acid (PubChem CID: 176),Adenosine 5′-triphosphate (PubChem CID: 5957),Bromelain,Carbohydrate moiety of bromelain (PubChem CID: 442,Carbon tetrachloride (PubChem CID: 5943),Eosin (PubChem CID: 11048),Ethylenediaminetetraacetic acid (PubChem CID: 6049,Hematoxylin (PubChem CID: 442514),Maleic acid (PubChem CID: 444266),Myofibrillar protein,Ninhydrine (PubChem CID: 10236),Papain,Paraformaldehyde (PubChem CID: 712),Squid,Tenderization,Trichloroacetic acid (PubChem CID: 6421),Trihydroxymethyl aminomethane (PubChem CID: 870730},
pages = {108991},
pmid = {32247462},
publisher = {Elsevier Ltd},
title = {{The mechanistic effect of bromelain and papain on tenderization in jumbo squid (Dosidicus gigas) muscle}},
url = {https://doi.org/10.1016/j.foodres.2020.108991},
volume = {131},
year = {2020}
}
@article{Kartika2019,
abstract = {Meat quality for the community is determined by the level of tenderizer. The process of meat tenderization could be done by giving papain enzymes derived from papaya fruit or leaves. Meat with the administration of papain enzymes can be analyzed based on protein profiles to see protein and microstructural integrity to see the texture of meat. The research sample was 20 g of beef and goat's meat with the treatment using the enzyme papain derived from papaya leaves. Time variation of enzyme administration 1 h, 2 h, 4 h, and 8 h, as well as variations in the weight of crude papain extract from papaya leaves as much as 10 g, 15 g, and 20 g. Analysis of protein concentration using Bradford and Kjeldhal methods, and protein profiles using the SDS PAGE method, and microstructural analysis using SEM. The concentration of meat protein with the treatment of crude extract of papaya leaves decreased compared to control meat. Based on protein profile analysis showed that meat given the enzyme papain from papaya leaves experienced protein band loss at a size of 225 kDa, 150 kDa, 96 kDa, 86 kDa. Microstructural analysis showed that beef and goat's meat treated with damage to collagen fibers, collagen fibers did not stick with muscle fibers, and the arrangement was irregular, in addition, there was a distance between muscle fibers.},
author = {Kartika, A. I. and Kusuma, H. S. and Darmawati, S. and Tanjung, D. S.},
doi = {10.1088/1755-1315/292/1/012010},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/Kartika_2019_IOP_Conf._Ser.__Earth_Environ._Sci._292_012010.pdf:pdf},
issn = {17551315},
journal = {IOP Conference Series: Earth and Environmental Science},
keywords = {meat microstructural,meat tenderizer,papain enzyme,proteomic analysis},
number = {1},
title = {{Microstructural and proteomic analysis to investigate the effectiveness of papaya leaf as a tenderizer of beef and goat's meat}},
volume = {292},
year = {2019}
}
@article{Lambri2014,
abstract = {Proteases are protein digesting biocatalysts long time used in the food industry. Although many authors reported the crystallization of papain and chymopapain from papaya latex, the powder of crude papain had the largest application as food supplements due to its highly positive effect on the degradation of casein and whey proteins from cow's milk in the stomach of infants. As the industrial preparative procedures have not been extensively applied, this study aims at producing dehydrated crude papain from fresh papaya pulp, planning lab-scale trials, followed by process development toward the pilot industrial-scale. In the lab-scale experiments, the enzyme activity (EA), expressed as protease unit (PU) /g, were evaluated on pulp and papain standard before and after a 2 h thermal treatment at 70 °C, 90 °C, and 120 °C, and the thermal behavior was monitored by means of differential scanning calorimeter (DSC). The process development toward the pilot-scaling optimized: the homogenization of the fresh pulp, followed by its filtration at high pressure (HP) in order to obtain the vegetation water and the pre-dehydrated pulp which was then oven dried varying the time-temperature conditions (4 h-80 °C; 2 h-120 °C; 30 min-150 °C). Proceeding at higher temperatures for a shorter time allowed obtaining commodity-related and technologically valid products. In the final pilot-scale step, filtration was done with vertical HP filter press, and final dehydration was performed with 2-step turbo-drying: the first aimed to concentrate with 2 min air flow (500 m3/h) at 200 °C, the second aimed to dry with 10 min air flow (500 m3/h) at 120 °C. The resulting dehydrated pulp was grinded with ball-mill to obtain a stable powder. Starting from 90±2 % pulp moisture, the two turbo-drying steps lowered the water content from 75±4 % to 50±2 % and from 50±2 % to 8±1 %, respectively. The enzyme release from the final powder highlighted an EA of the food-grade crude papain powder extract of 28 PU/g. The thermal steps provided with turbo-driers permitted to maintain a fraction of sugars and pectin acting as a protective structure, so increasing the digestion effects provided by papain. Vegetation waters were ultra-filtered allowing at obtaining a concentrated pectin suspension and rich in nutrient waters which can be reused along the food chain. Further efforts should be made to implement this procedure as potential alternative for the dehydrated crude papain production, deepening the impact of process variables on this matter. {\textcopyright} 2014, AIDIC Servizi S.r.l.},
author = {Lambri, Milena and Roda, Arianna and Dordoni, Roberta and Fumi, Maria Daria and {De Faveri}, Dante Marco},
doi = {10.3303/CET1438002},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/002.pdf:pdf},
isbn = {9788895608297},
issn = {22839216},
journal = {Chemical Engineering Transactions},
number = {June},
pages = {7--12},
title = {{Mild process for dehydrated food-grade crude papain powder from papaya fresh pulp: Lab-scale and pilot plant experiments}},
volume = {38},
year = {2014}
}
@article{Lukin2020,
abstract = {Protepsin belongs to the class of acid proteinases, containing carboxyl groups in the active center. The preparation cleaves peptide bonds formed by aromatic amino acids (tyrosine, phenylalanine), and does not hydrolize esters and amides. Along with the proteolytic complex, Protepsin contains collagenase, lipase, and other digestive enzymes. The preparation is obtained according to the original technology through maceration of animal endocrine raw materials, followed by purification, concentration, isolation and freeze dehydration of the enzyme complex. The results of the laboratory studies of the proteolytic activity of enzyme preparations show that Protepsin, the preparation of animal origin with a proteolytic activity of 100 units/g, has the greatest collagenase activity in the biomodification of native collagen-containing raw materials.},
author = {Lukin, Aleksandr},
doi = {10.1590/fst.09319},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/0101-2061-cta-fst09319.pdf:pdf},
isbn = {9219005427892},
issn = {1678457X},
journal = {Food Science and Technology},
keywords = {Cattle by-products,Enzyme preparations,Protein hydrolysate,Proteolytic activity,Protepsin},
number = {June},
pages = {287--292},
title = {{Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates}},
volume = {40},
year = {2020}
}
@book{Meshram2018,
abstract = {Enzymes are highly specific biological catalysts involved in food biotechnology. Enzyme production and application in the food manufacturing industry are based on a profound understanding of the enzyme's in traditional foods. Plant-derived enzymes include amylase, invertase, papain, bromelain, ficin, lipoxygenase, etc. These enzymes have played an important part in food production, for example, syrups, bakery products, alcoholic beverages, dairy products, etc. Besides the use of plants as a factory for enzyme production in the food industry, they can also serve as raw material (enhancer) for the enhancement of microbial enzyme activity employed in the food industry. New approaches such as direct genetic modification are now in progress that might significantly contribute to the improvement of the nutritional value of plant-derived foods or the quality of food using enzymes derived from plant sources. Earlier enzymes were isolated from living cells (plants and animals), which led to their large-scale commercial production and wider application in the food industry. Today, microorganisms are the most important source of commercial enzymes. However, the safety of the source organism is the primary consideration in assessing an enzyme product. Food animals and edible plants have a history of safe use as sources of enzymes for the food industry.},
author = {Meshram, Anju and Singhal, Gauri and Bhagyawant, Sameer S. and Srivastava, Nidhi},
booktitle = {Enzymes in Food Biotechnology: Production, Applications, and Future Prospects},
doi = {10.1016/B978-0-12-813280-7.00028-1},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/B978-0-12-813280-7.00028-1.pdf:pdf},
isbn = {9780128132807},
keywords = {Antinutritional factors,Food biotechnology,Invertase,Papain,Plant-derived enzymes},
pages = {483--502},
publisher = {Elsevier Inc.},
title = {{Plant-derived enzymes: A treasure for food biotechnology}},
url = {https://doi.org/10.1016/B978-0-12-813280-7.00028-1},
year = {2018}
}
@article{Moczkowska2017,
abstract = {The aim of this study was to evaluate the impact of the ageing on changes in selected myofibrillar proteins and Warner–Bratzler shear force values in muscles from cross-breed Charolaise × Holstein Friesian heifers. Triceps brachii (TB), infraspinatus (IS), vastus lateralis (VL), semimembranosus (SM), biceps femoris (BF) and semitendinous (ST) muscles after ageing were examined. A significant muscle effect was found in the case of basic chemical composition, Warner–Bratzler shear force values and cooking loss. The vastus lateralis characterised by the lowest intramuscular fat percentage (P ≤ 0.05). The highest connective tissue content was shown for infraspinatus. This muscle had the lowest Warner–Bratzler shear force values in every ageing time, regardless of the cooking method. Throughout the ageing process, selected myofibrillar proteins were altered in all examined muscles, but at varying rates. The SDS-PAGE electrophoresis and Western blotting analysis showed that desmin and troponin-T degradation affected both muscles and ageing effects (P ≤ 0.001).},
author = {Moczkowska, Ma{\l}gorzata and P{\'{o}}{\l}torak, Andrzej and Wierzbicka, Agnieszka},
doi = {10.1111/ijfs.13436},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/ijfs.13436.pdf:pdf},
issn = {13652621},
journal = {International Journal of Food Science and Technology},
keywords = {Beef,electrophoresis SDS-PAGE,muscle,protein degradation,tenderness},
number = {6},
pages = {1375--1382},
title = {{The effect of ageing on changes in myofibrillar protein in selected muscles in relation to the tenderness of meat obtained from cross-breed heifers}},
volume = {52},
year = {2017}
}
@article{Monti2000,
abstract = {In the present study we wish to report a method of crystallizing papain from fresh papaya latex which gave higher yields than previously reported. This method does not involve the use of sulphydryl reagents. The papain thus obtained is practically pure and shows a single band when submitted to electrophoresis on polyacrylamide gel, and is identical to the papain obtained by other methods. In routine enzymatic assays, specific activity was measured using Z-gly-pNP and BAEE as substrates. Papain crystallized by this method, without the use of high concentrations of salts or thiol-containing substances such as cysteine and dithiothreitol, is obtained in the form of a complex with natural inhibitors existent in latex which can be removed by dialysis.No presente trabalho apresenta-se um m{\'{e}}todo de cristaliza{\c{c}}{\~{a}}o da papa{\'{i}}na oriunda do l{\'{a}}tex fresco de mam{\~{a}}o, o qual apresenta uma alta produtividade em rela{\c{c}}{\~{a}}o aos m{\'{e}}todos previamente descritos. A metodologia aqui descrita n{\~{a}}o envolve o uso de reagentes sulfidr{\'{i}}licos, a papa{\'{i}}na foi obtida de forma praticamente pura, apresentando uma simples banda quando submetida a eletroforese, e com propriedades id{\^{e}}nticas {\`{a}}quelas obtidas por outros m{\'{e}}todos. A atividade espec{\'{i}}fica foi determinada utilizando Z-gly-pNP e BAEE como substrato. A papa{\'{i}}na obtida por essa metodologia, sem uso de subst{\^{a}}ncias tais como ciste{\'{i}}na e ditiotreitol, apresenta-se na forma de um complexo com inibidores naturais, os quais podem ser removidos por di{\'{a}}lise.},
author = {Monti, Rubens and Basilio, Carmelita A. and Trevisan, Henrique C. and Contiero, Jonas},
doi = {10.1590/s1516-89132000000500009},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/a08v43n5.pdf:pdf},
issn = {1678-4324},
journal = {Brazilian Archives of Biology and Technology},
keywords = {carica papaya,cysteine proteinase,papain,proteolytic enzymes,purification of papain},
number = {5},
pages = {501--507},
title = {{Purification of papain from fresh latex of Carica papaya}},
volume = {43},
year = {2000}
}
@article{Ningrum2018,
abstract = {Papain (E.C.3.4.22.2) is a proteolytic enzyme which has important role due toits diverse uses in textile, pharmaceutics, cosmetics and food industries.Papain enzyme can be found in almost all parts of the papaya plant and mostof the stem and fruit. The objective of this study is to compare the Californiavar. and Indonesian local var. of papaya fruits, in papain production and alsoto characterize the enzyme properties. Results showed that the highest yield ofcrude papain was obtained from local papaya latex (24.87%) whichprecipitated by ethanol with ratio of 1:2. The highest of activity enzyme,soluble protein and specific enzyme activity obtained from the local papayawere 3154 ± 11.31unit/mL, solubility protein of 0.94± 0.08 mg/mL andspesific enzyme activity of 3355.32 unit/mg protein, respectively. The activityof enzyme fraction F7 obtained from purification by DEAE sepharose columnwas 202.33 U/mL dan the molecular weight of this fraction was between 17-28 kDa.{\textcopyright} 2},
author = {Ningrum, Diah Ratna and Kosasih, Wawan and Priatni, Sri},
doi = {10.14203/jkti.v19i2.242},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/242-921-1-PB.pdf:pdf},
issn = {0853-2788},
journal = {Jurnal Kimia Terapan Indonesia},
keywords = {california var,isolation,latex,local var,papaya,protease enzyme},
number = {2},
pages = {42--48},
title = {{The Comparative Study of Papain Enzyme from Papaya Fruits California variant and Indonesian Local variant}},
volume = {19},
year = {2018}
}
@article{Ranatunga2018,
abstract = {Observations made in temperature studies on mammalian muscle during force development, shortening, and lengthening, are re-examined. The isometric force in active muscle goes up substantially on warming from less than 10°C to temperatures closer to physiological (>30°C), and the sigmoidal temperature dependence of this force has a half-maximum at $\sim$10°C. During steady shortening, when force is decreased to a steady level, the sigmoidal curve is more pronounced and shifted to higher temperatures, whereas, in lengthening muscle, the curve is shifted to lower temperatures, and there is a less marked increase with temperature. Even with a small rapid temperature-jump (T-jump), force in active muscle rises in a definitive way. The rate of tension rise is slower with adenosine diphosphate (ADP) and faster with increased phosphate. Analysis showed that a T-jump enhances an early, pre-phosphate release step in the acto-myosin (crossbridge) ATPase cycle, thus inducing a force-rise. The sigmoidal dependence of steady force on temperature is due to this endothermic nature of crossbridge force generation. During shortening, the force-generating step and the ATPase cycle are accelerated, whereas during lengthening, they are inhibited. The endothermic force generation is seen in different muscle types (fast, slow, and cardiac). The underlying mechanism may involve a structural change in attached myosin heads and/or their attachments on heat absorption.},
author = {Ranatunga, K. W.},
doi = {10.3390/ijms19051538},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/ijms-19-01538.pdf:pdf},
issn = {14220067},
journal = {International Journal of Molecular Sciences},
keywords = {Actin-myosin,Crossbridge cycle,Crossbridge force,Endothermic force,Muscle force,Muscle shortening,Temperature-sensitivity},
number = {5},
pmid = {29786656},
title = {{Temperature effects on force and actin-myosin interaction in muscle: A look back on some experimental findings}},
volume = {19},
year = {2018}
}
@article{Parkash2021,
author = {Parkash, Jai and Sharma, DP and Yadav, S},
doi = {10.22271/tpi.2021.v10.i3sd.5881},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/S-9-10-7-589.pdf:pdf},
issn = {23498242},
journal = {The Pharma Innovation},
keywords = {buffalo calf meat,ginger,natural tenderizers,natural tenderizers, papain, ginger, buffalo calf,papain},
number = {3S},
pages = {203--205},
title = {{Application of natural tenderizers (Papain and ginger) in buffalo calf meat}},
volume = {10},
year = {2021}
}
@article{Saeed2017,
abstract = {Papaya extract from Carica papaya (dwarf solo) was found to curtail active growth of Salmonella typhimurium. Four different segments of Carica papaya fruit were processed and protein concentration of unripen peel (48.7%), unripen latex (58.5%), ripe peel (40.5%) and ripe latex (50.7%) were observed. The protease activity and pH of extract of unripe latex, unripe peel, ripe latex and ripe peel were recorded as “1648 - 9.20”, “1684.5 - 9.91” and “5 - 4.5”, “6 - 4.7” respectively. The proteolytic activity of unripe and ripe peel extract was observed as 9.20 and 9.91 at pH 4.5 and 4.7. The proteolytic activity of unripe and ripe latex extract was observed as 1648 and 1680.5 at pH 5 and 6 respectively. Anti-Salmonella activity of papaya extract was accessed through multiple dilution technique to find out minimum inhibitory concentration. Papaya extract from ripe peel showed minimum 25.31µg of MIC50 and 50.62µg of MIC90, followed by unripe latex with MIC50 at 36.56µg and MIC90 at 73.12µg. However, the MIC50 for unripen peel was 60.93µg and MIC90 at 121.87µg likewise the papaya extract derived from ripe latex showed MIC50 at 63.37µg and MIC90 at 126.75µg. Ripe peel and unripen latex had better potential to control Salmonella typhimurium growth. The beef kababs incorporated with unripe latex extract at various levels (0, 0.5, 1.0, 1.5, 2.0, 2.5 and 3.0 mg/100g), showed significant reduction in moisture contents while protein, fat, ash, cooking yield and texture showed non-significant variation during storage.},
author = {Saeed, Muhammad and ur Rahman, Sajjad and Shabbir, Muhammad Asim and Khan, Nassrulla and Shakeel, Azam},
doi = {10.21162/PAKJAS/17.5032},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/2685 (1).pdf:pdf},
issn = {20760906},
journal = {Pakistan Journal of Agricultural Sciences},
keywords = {Beef kababs,Minimum inhibitory concentration,Papaya extract,Protease activity,Salmonella typhimorium},
number = {1},
pages = {153--159},
title = {{Extraction and utilization of Papaya extract as meat tenderizer and antimicrobial activity against Salmonella typhimurium}},
volume = {54},
year = {2017}
}
@article{Soji2020,
author = {Soji, Zimkhitha and Chulayo, Amanda Yucca},
doi = {10.5713/ajas.20.0154},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/ajas-20-0154.pdf:pdf},
isbn = {2786628296},
issn = {1011-2367},
journal = {Asian-Australasian Journal of Animal Sciences},
keywords = {muscle fibre diameter,muscle fibre spacing,myofibril diameter,myofibril spacing,sarcomere length},
number = {00},
pages = {1--11},
title = {{Beef tenderness evaluation using early post-mortem muscle nanostructure}},
volume = {00},
year = {2020}
}
@article{Sukada2019,
abstract = {This research was conducted at the Laboratory of Animal Produce Technology Faculty of Veterinary, Udayana University. Aims to determine the effect of papaya leaf extract, extract pineapple and ginger extract on the physical and organoleptic qualities of Bali beef through soaking. Variables measured to determine the physical properties of meat between meat pH and shrinkage of cooked meat, while the variables measured to determine the organoleptic quality of Bali beef among other examples: color, texture, taste, and smell of meat by panelist. The analyze used variance analysis, while experiment design used in this research is, Completely Random Design simple 4 treatment pattern 5 replication from Steel and Torie processed by Costas Statistic Method. Measurement of pH of the meat using pH meters, and the measurement of moisture content after cooking, is sought through the calculation of the percentage ratio of the difference between the weight of raw meat and the weight of meat after cooking. Conclusions and results of this study found that beef soaked in pineapple extracts showed: raw shrinkage, texture, color, taste, tenderness, and odor showed the best physical and organoleptic quality (P <0.05) compared to ginger extract and papaya leaf extract. While the physical and organoleptic qualities of beef soaked in extra papaya leaves show the worst indication.},
author = {Sukada, I Ketut and Suberata, I Wayan and Rasna, Ni Made Artiningsih},
doi = {10.29332/ijls.v3n1.241},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/600912d799d1a332e8422edf08c64b31f5da.pdf:pdf},
issn = {2550-6994},
journal = {International journal of life sciences},
number = {1},
pages = {12--24},
title = {{Immersion effect with extracts of papaya leaf, pineapple, ginger on quality of organoleptic and Bali beef nutrition}},
volume = {3},
year = {2019}
}
@article{Suleman2020,
abstract = {Lamb meat is cooked using different methods which help to impart good taste, flavour and aroma and they also improve the nutritional quality and ensure food safety. However traditional methods also induce some potential health hazards i.e. formation of polyaromatic hydrocarbons, heterocyclic aromatic amines and acrylamides. These harmful compounds are produced through protein aggregation (protein increased with loss of water), lipid degradation (lipid breakdown due to cooking), oxidation (radicals formation due to heat and oxygen combination), and the Maillard reaction (reaction between sugars and amino acids). This review focuses on: 1) the use of modern cooking technologies to reduce the generation of hazardous compounds by a) applying low temperature cooking with minimum contact with the meat; b) faster cooking, with the added benefits of minimum nutritional losses and less energy consumption 2) the adoption of natural plant sources as extracts to: a) inhibit lipid oxidation; b) improve the stability of meat products to limit the generation of hazardous compounds.},
author = {Suleman, Raheel and Wang, Zhenyu and Aadil, Rana Muhammad and Hui, Teng and Hopkins, David L. and Zhang, Dequan},
doi = {10.1016/j.meatsci.2020.108172},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/1-s2.0-S0309174019309088-main.pdf:pdf},
issn = {03091740},
journal = {Meat Science},
keywords = {Cooking,Hazards,Lamb meat,Novel technologies,Quality},
number = {1},
pages = {108172},
pmid = {32422547},
publisher = {Elsevier},
title = {{Effect of cooking on the nutritive quality, sensory properties and safety of lamb meat: Current challenges and future prospects}},
url = {https://doi.org/10.1016/j.meatsci.2020.108172},
volume = {167},
year = {2020}
}
@article{Vikhlyantsev2017,
abstract = {Almost 40 years has passed since the discovery of giant elastic protein titin (also known as connectin) of striated and smooth muscles using gel electrophoresis. Sodium dodecyl sulfate polyacrylamide gel electrophoresis is a major technique for studying the isoform composition and content of titin. This review provides historical insights into the technical aspects of the electrophoresis methods used to identify titin and its isoforms. We particularly focus on the nuances of the technique that improve the preservation of its primary structure so that its high molecular weight isoforms can be visualized.},
author = {Vikhlyantsev, Ivan M. and Podlubnaya, Zoya A.},
doi = {10.1007/s12551-017-0266-6},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/12551_2017_Article_266.pdf:pdf},
issn = {18672469},
journal = {Biophysical Reviews},
keywords = {SDS-Page,Striated muscles,Titin isoforms,Titin/connectin},
number = {3},
pages = {189--199},
publisher = {Biophysical Reviews},
title = {{Nuances of electrophoresis study of titin/connectin}},
volume = {9},
year = {2017}
}
@article{Welde2018,
abstract = {Papain is a proteolytic enzyme currently in papaya that breaks down proteins and widely it has a dozens of food processing applications. Generally, the objective of this study was to extract papain enzyme by different extraction technique mainly using grinding method and ultrasonication. Experimental study was conducted from February 2017-May 2017. The collection of fresh papaya leaf was taken from locally grown papaya from Adigrat in region of Tigray by using cutting and then it was taken in molecular laboratory of Biotechnology department. By using the reagent for purification of the extracted papain was done by using ammonium sulfate and sodium chloride precipitation. The concentration of enzyme was then determined by Bradford method. The enzyme for pyrolytic activity was determined according to the procedure of Arnon with some addition of modifying his manual. The concentration of extract papain was from 0.055-0.003 mg/ml. The maximum mean value was shown by the grinded sample and the minimum mean concentration was 0.003 obtained from the sonicated sample within temperature of 50 0 C for 25min. The maximum mean absorbance for enzyme activity was shown by sonicated sample at 1h by 60 0 c and the minimum mean absorbance was from the sonicated sample within temperature of 50 0 C for 20min. Finally, papaya leaves contain papain enzyme, and this needs further the widest application of prosecuting research.},
author = {Welde, Yidnekachew and Worku, Abebe},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/6-2-50-380.pdf:pdf},
issn = {2394-0530},
journal = {Journal of Medicinal Plants Studies},
keywords = {Carica papaya,Papain,Proteolytic Enzymes},
number = {3},
pages = {127--130},
title = {{Identification and extraction of papain enzyme from papaya leaf in adigrat towen, northern Ethiopia}},
volume = {6},
year = {2018}
}
@article{Yu2020,
abstract = {In this work, the effect of adding different quaternary ammonium ionic liquids (ILs) on the phase formation behaviour of a PEG400+(NH4)2SO4+H2O aqueous two-phase system (ATPS) and separation and purification of crude papain extract from papaya latex in different ATPSs was studied. Phase diagrams were established for different systems: experimental phase diagram data were fitted by the Merchuk equation, and the tie line (TL), composition and tie line length (TLL) were determined. The papain purification effect of ATPSs with various ILs was systematically scrutinized. The absorption spectrum of papain before and after extraction was characterized by UV-vis absorption spectroscopy. SDS-PAGE electrophoresis was used to verify the purity of papain extracted by the ATPSs. Quaternary ammonium ILs as adjuvants did not extend the biphasic area in the phase diagram, but the partition behaviour of crude papain extract in ATPSs changed, resulting in additional IL and papain interactions that promoted papain purification. The highest papain purity was obtained when tetramethyl ammonium bromide ([N1111]Br) was added to the ATPS, and with 20 wt% (NH4)2SO4 and 20 wt% PEG400 at pH 7.0 and 60 °C, the purification factor of crude papain extract was 2.13 and 13.51 and the papain recovery rate was 64.2% and 96.46% for ATPSs with no IL and 4 wt% [N1111] Br, respectively. The UV spectra of papain before and after extraction were the same. The SDS-PAGE analysis revealed that the ATPS containing 4 wt% [N1111] Br enhanced papain purification relative to the ATPS without IL. The addition of 4 wt% IL greatly improved the purification factor of crude papain extract enriched in the PEG phase, providing a potential method for large-scale industrial production of high-purity papain.},
author = {Yu, Lei and Zhang, Haide},
doi = {10.1007/s12161-020-01761-z},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/s12161-020-01761-z.pdf:pdf},
issn = {1936976X},
journal = {Food Analytical Methods},
keywords = {Adjuvant,Aqueous two-phase system,Ionic liquids,Papain,Separation and purification},
number = {7},
pages = {1462--1474},
publisher = {Food Analytical Methods},
title = {{Separation and Purification of Papain Crude Extract from Papaya Latex Using Quaternary Ammonium Ionic Liquids as Adjuvants in PEG-Based Aqueous Two-Phase Systems}},
volume = {13},
year = {2020}
}
@article{Zapata2009,
abstract = {Inconsistent tenderness is one of the most detrimental factors of meat quality. Functional proteomics was used to associate electrophoretic bands from the myofibrillar muscle fraction to meat tenderness in an effort to gain understanding of the mechanisms controlling tenderness. The myofibrillar muscle fraction of the Longissimus dorsi from 22 Angus cross steers was analyzed by SDS-PAGE and linearly regressed to Warner-Bratzler shear values. Six significant electrophoretic bands were characterized by electrophoretic and statistical analysis and sequenced by nano-LC-MS/MS. The protein(s)/peptide(s) identified in these bands encompass a wide array of cellular pathways related to structural, metabolic, chaperone, and developmental functions. This study begins to assemble information that has been reported separately into a more complete picture that will lead to the establishment of a coherent mechanism accounting for meat tenderness. {\textcopyright} 2009 American Chemical Society.},
author = {Zapata, Isain and Zerby, Henry N. and Wick, Macdonald},
doi = {10.1021/jf900041j},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/Functional_Proteomic_Analysis_Predicts_B20160126-28427-q856k2-with-cover-page.pdf:pdf},
issn = {00218561},
journal = {Journal of Agricultural and Food Chemistry},
keywords = {Beef,Longissimus dorsi,Proteomlcs,Tenderness},
number = {11},
pages = {4956--4963},
pmid = {19449808},
title = {{Functional proteomic analysis predicts beef tenderness and the tenderness differential}},
volume = {57},
year = {2009}
}
@article{Onopiuk2019,
abstract = {The aim of the study was to define the influence of small-molecule proteins originating from the degradation of troponin T and intensity of fluorescence spectra on the tenderness of the Semitendinosus (ST) and Infraspinatus (IS) muscles, and determining their interdependence with instrumentally measured Warner-Bratzler Shear Force (WBSF). The examined muscles, sampled from Limousin × Holstein-Friesian beef crossbreds differed to a statistically significant extent (p<0.05) in the length of the sarcomeres, content of protein, fat, and total collagen. An increase in the activity of proteins originating from the process of degradation of troponin T was highly correlated with the WBSF both in the case of the ST (r2=0.851) and IS (r2=0.765) muscle. The 305÷400 nm emission spectrum, recorded with front-face fluorescence spectroscopy made it possible to calculate the intensity of fluorescence of tryptophan residues. The studies proved a relationship between the WBSF and intensity of tryptophan residues fluorescence on the level of r2=0.682 (ST) and r2=0.714 (IS).},
author = {Onopiuk, Anna and P{\'{o}}{\l}torak, Andrzej and Wierzbicka, Agnieszka},
file = {:Users/muchamaddafip/Documents/KERJAAN/FEMALE /APRILIA/REF. PAPAIN APRIL/ContentServer.pdf:pdf},
issn = {23008342},
journal = {Animal Science Papers and Reports},
keywords = {Beef,Fluorescence spectroscopy,Muscles,SDS-PAGE,Tenderness,Tryptophan},
number = {3},
pages = {243--258},
title = {{Changes in chemical composition and tenderness of selected beef muscles during aging analysed with sds-page and fluorescence spectroscopy}},
volume = {37},
year = {2019}
}