Characterization of Fish Skin Hydrolysates Exhibiting Dipeptidyl Peptidase IV Inhibitory Activity

https://doi.org/10.22146/ifnp.88534

Honoka Miyamoto(1), Erwina Safitri(2), Takeshi Nagai(3), Masataka Saito(4*)

(1) Kagawa Nutrition University
(2) Kagawa Nutrition University
(3) Yamagata University
(4) Kagawa Nutrition University
(*) Corresponding Author

Abstract


Dipeptidyl peptidase IV (DPP-IV) inhibitors are antidiabetic drugs that can lower blood sugar levels. There are still few reports on the DPP-IV inhibitory activity of peptides obtained from discarded fish skin. Therefore, we prepared various enzymatic hydrolysates using the skins of six fish species and investigated their DPP-IV inhibitory effects. As a result, it was found that the DPP-IV inhibitory activity of yellowtail hydrolysate by Alcalase was higher than that of other enzymes. In addition, the IC50 after ethanol fractionation was found to be lower in yellowtail and eel skin hydrolysate. Amino acid composition analysis showed that the hydrolysate obtained from the skin of the yellowtail contained the highest amount of Gly, followed by Pro, Hyp, and Ala, indicating that it was a peptide derived from type I collagen. Fractionation with ethanol showed that the DPP-IV inhibitory components were contained in the low molecular weight fraction. The artificial digestion test observed no DPP-IV inhibitory activity or average molecular weight change. The DPP-IV inhibitory peptide obtained from fish skin has the potential to be applied as a food material to various food products.


Keywords


Alcalase; Collagen hydrolysate; Dipeptidyl Peptidase Ⅳ (DPP-Ⅳ); Fish skin

Full Text:

PDF


References

Agustia, F., C., Murdiati, A., Supriyadi, Indrati, R. (2023). Production of Dipeptidyl Peptidase-IV Inhibitory Peptides from Germinated Jack Bean [Canavalia ensiformis (L.) DC.]. Flour. Prev. Nutr. Food Sci., 28(2), 149-159

David, R., Jennifer L. (2020). Skin collagen through the life stages: Importance for skin health and beauty. Plast. Aesthet. Res., 153, 1-24

Desai, S., Brinker, A., Swann, J., Iyasu, S. (2010). Sitagliptin-associated drug allergy: Review of spontaneous adverse event reports. Arch. Intern. Med., 170, 1169–1171

Doucet, D., Otter, D., Gauthier, S. F., Foegeding, E. A. (2003). Enzyme-induced gelation of extensively hydrolyzed whey proteins by Alcalase: Peptide identification and determination of enzyme specificity. J. Agric. Food Chem., 51, 6300-6308

Gheni, G., Ogura, M., Iwasaki, M., Yokoi, N., Minami, K., Nakayama, Y., Harada, K., Hastoy, B., Wu, X., Takahashi, H., Kimura, K., Matsubara, T., Hoshikawa, R., Hatano, N., Sugawara, K., Shibasaki, T., Inagaki, N., Bamba, T., Mizoguchi, A., Fukusaki, E., Rorsman, P., Seino, S. (2014). Glutamate acts as a key signal linking glucose metabolism to incretin/cAMP action to amplify insulin secretion. Cell Rep., 9, 661-673

Güntelberg, A., V., Ottesen, M. (1952). Preparation of crystals containing the albumin-forming enzyme from Bacillus subtilis. Nature, 170, 802-802

Hatanaka, T., Kawakami, K., Uraji, M. (2014). Inhibitory effect of collagen-derived tripeptides on dipeptidyl peptidase-IV activity. J. Enzyme Inhib. Med. Chem., 29, 823-828

He, L., Wang, X., Wang, Y., Luo, J. (2023). Production and identification of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from discarded cowhide collagen. Food Chem., 405, 134793

Hsu, K.-C., Tung, Y.-S., Huang, S.-L., & Jao, C.-L. (2013). Dipeptidyl peptidase-IV inhibitory activity of peptides in porcine skin gelatin hydrolysates. Food Microbiol., 10, 205-218

Jia, C. L., Hussain, N., Joy Ujiroghene, O., Pang, X. Y., Zhang, S. W., Lu, J., Liu, L., & Lv, J. P. (2020). Generation and characterization of dipeptidyl peptidase-IV inhibitory peptides from trypsin-hydrolyzed α-lactalbumin-rich whey proteins. Food Chem., 318, 126333

Jin, R., Teng, X., Shang, J., Wang, D., Liu, N. (2020). Identification of novel DPP–IV inhibitory peptides from Atlantic salmon (Salmo salar) skin. Food Res. Int., 133, 109161

Kimura, S., Saito, M. (1999). Collagen in edible fish its biochemical properties in comparison with those of mammals. In Kenji S., Morihiko S., and H. Allan B. (Eds.). Characterization of fish type I collagen in extracellular matrix of fish and shellfish. (pp.1-13). Research Signpost (Trivandrum India).

Kumar, C., G., Takagi, H. (1999). Microbial alkaline proteases: from a bioindustrial viewpoint. Biotechnol., 17, 561-594

Kong, X., Zhang, L., Song, W., Zhang, C., Hua, Y., Chen, Y., Li, X. (2021). Separation, identification, and molecular binding mechanism of dipeptidyl peptidase IV inhibitory peptides derived from walnut (Juglans regia L.) protein. Food Chem., 347, 129062

Lacroix, M., Li-Chan, E. (2012). Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. Int. Dairy J., 2, 97-102

Lacroix, M., Li-Chan, E. (2013). Inhibition of dipeptidyl peptidase (DPP)-IV and α-glucosidase activities. J. Agric. Food Chem., 61, 7500–7506

Liu, R., Cheng, J., Wu, H. (2019). Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review Int. J. Mol. Sci., 20, 463

Liu, W., Wang, X., Yang, W., Li, X., Qi, D., Chen, H., Liu, H., Yu, S., Pan, Y., Liu, Y., Wang, G. (2022). Identification, screening, and comprehensive evaluation of novel DPP-IV inhibitory peptides from the tilapia skin gelatin hydrolysate produced using ginger protease. Biomolecules, 12, 1866

Li-Chan, E. C., Hunag, S. L., Jao, C. L., Ho, K. P., Hsu, K. C. (2012). Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors. J. Agric. Food Chem., 60, 973–978

Nonaka, K., Kakikawa, T., Sato, A., Okuyama, K., Fujimoto, G., Kato, N., Suzuki, H., Hirayama, Y., Ahmed, T., Davies, M. J., Stein, P. P. (2008). Efficacy and safety of sitagliptin monotherapy in Japanese patients with type 2 diabetes. Diabetes Res. Clin. Pract., (79), 291–298

Nongonierma, A. B. and FitzGerald, J. R. (2013). Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing casein-derived peptides. J. Funct. Foods, 5, 1909-1917

Nongonierma, A. B., Paolella, S., Mudgil, P., Maqsood, S. (2018). Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel milk protein hydrolysates. Food Chem., 244, 340-348

Nong, N. T. P., Chen, Y. K., Shih, W. L., Hsu, J. L. (2013). Characterization of novel dipeptidyl peptidase-IV inhibitory peptides from soft-shelled turtle yolk hydrolysate using orthogonal bioassay-guided fractionations coupled with in vitro and in silico study. Pharmaceuticals, 10, 308-329

Saito, M., Higuchi, T., Uchida, N. (2014). Identification and primary structures of eel type I collagen proa1, proa2, and proa3. Fish. Sci., 80, 1323-1335

Smith, E., L. (1968). The complete sequence: Comparison with subtilisin BPN'; evolutionary relationship. J. Biol. Chem., 243, 2184-2191

Smushkin, G., Vella, A. (2009). Inhibition of dipeptidyl peptidase-4: The mechanism of action and clinical use of vildagliptin for the management of type 2 diabetes. Diabetes Metab. Syndr. Obes., 2, 83-90

Takahashi, Y., Kamata, A., Konishi, T. (2021). Dipeptidyl peptidase‑IV inhibitory peptides derived from salmon milt and their effects on postprandial blood glucose level. Fish. Sci., 87, 619-626

Theodosios, D., F., Vasilios, G., A., Moses, S., E. (2014). The pharmacokinetic considerations and adverse effects of DPP-4 inhibitors. Expert. Opin. Drug Metab. Toxicol., 6, 787-812

Thoma, R., Löffler, B., Stihle, M., Huber, W., Ruf, A., Hennig, M. (2003). Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure, 8, 947-959

Umezawa, H., Aoyagi, T., Ogawa, K., Naganawa, H., Hamada, M., Takeuchi, T. (1984). Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria. J. Antibiot., 37, 422-425

Wang, B., Yu, Z., Yokoyama, W., Chiou, B., Chen, M., Liu, F., Zhong, F. (2021). Collagen peptides with DPP-IV inhibitory activity from sheep skin and their stability to in vitro gastrointestinal digestion. Food Biosci., 42, 101161

Zhang, Y., Chen, R., Chen, X., Zeng, Z., Ma, H., & Chen, S. (2016). Dipeptidyl peptidase IV-inhibitory peptides derived from silver carp (Hypophthalmichthys molitrix Val.) Proteins. J. Agric. Food Chem., 4, 831-839

Zhuang, Y., Sun, L., Zhang, Y., Liu, G. (2012). Antihypertensive effect of long-term oral administration of jellyfish (Rhopilema esculentum) collagen peptides on renovascular hypertension. Mar. Drugs, 10, 417-426



DOI: https://doi.org/10.22146/ifnp.88534

Article Metrics

Abstract views : 315 | views : 234

Refbacks

  • There are currently no refbacks.


Creative Commons License
This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.

Indonesian Food and Nutrition Progress (print ISSN 0854-6177, online ISSN 2597-9388) is published by the Indonesian Association of Food Technologist in collaboration with Department of Food and Agricultural Product Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada.

Journal of Indonesian Food and Nutrition Progress have been indexed by: 

   

 

This works is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.