PRODUCTION AND CHARACTERIZATION OF CHITINASE ENZYMES FROM SULILI HOT SPRING IN SOUTH SULAWESI, Bacillus sp. HSA,3-1a

https://doi.org/10.22146/ijc.21470

Hasnah Natsir(1*), Abd. Rauf Patong(2), Maggy Thenawidjaja Suhartono(3), Ahyar Ahmad(4)

(1) Department of Chemistry, Faculty of Mathematics and Natural Sciences, Hasanuddin University, Jl. Perintis Kemerdekaan Km 10 Tamalanrea, Makassar 90245, South Sulawesi
(2) Department of Chemistry, Faculty of Mathematics and Natural Sciences, Hasanuddin University, Jl. Perintis Kemerdekaan Km 10 Tamalanrea, Makassar 90245, South Sulawesi
(3) Departement of Food Technology and Human Nutrition FATETA and Research Center for Biotechnology, Bogor Agricultural University, Jl. Raya Darmaga, Campus IPB, PO.BOX 220, Bogor 16002, West Java
(4) Department of Chemistry, Faculty of Mathematics and Natural Sciences, Hasanuddin University, Jl. Perintis Kemerdekaan Km 10 Tamalanrea, Makassar 90245, South Sulawesi
(*) Corresponding Author

Abstract


Chitinase is an extracellular enzyme which is capable in hydrolyzing insoluble chitin to its oligomeric and monomeric components. The enzyme produced by thermophilic bacteria was screened and isolated from Sulili hot spring in Pinrang, South Sulawesi, Indonesia. The gram positive spore forming rod shape bacteria was identified as Bacillus sp. HSA,3-1a through morphological and physiological analysis. The production of chitinase enzyme was conducted at various concentration of colloidal chitin at a pH of 7.0 and a temperature of 55 °C. The bacteria optimally was produced the enzyme at a colloidal chitin concentration of 0.5% after 72 h of incubation. The optimum temperature, pH and substrate concentration of chitinase were 60 °C, 7.0 and 0.3%, respectively. The enzyme was stable at a pH of 7.0 and a temperature of 60 °C after 2 h of incubation. The chitinase activities was increased by addition of 1 mM Mg2+, Ca2+ and Mn2+ ions, whereas the activities were decreased by 1 mM Co2+, Fe2+ andZn2 ions. The molecular weight of the crude enzyme was determined using SDS-PAGE analysis. Five protein fractions were obtained from SDS-PAGE, with MWs of 79, 71, 48, 43 and 22 kDa.

 

Keywords: colloidal chitin, thermophilic bacteria, chitinase

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DOI: https://doi.org/10.22146/ijc.21470

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Indonesian Journal of Chemisty (ISSN 1411-9420 / 2460-1578) - Chemistry Department, Universitas Gadjah Mada, Indonesia.

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