PRODUCTION OF PROTEASE ENZYME FROM BACTERIA IN HOT SPRING OF SOUTH SULAWESI, Bacillus licheniformis HSA3-1a
DOI:
https://doi.org/10.20956/mca.v16i1.949Abstract
Bacillus licheniformis HSA3-1a is able to produce extracellular protease. The aim of this research was to find out its production optimum time, consentration of MnCl2, temperature and optimum pH, also the cofactor influence on activity protease from B. licheniformis HSA3-1a. The protease activity was tested with a modified method of Walter. Protease production time was optimum for 36 hours with an activity value of 0,394 U/mL, protein content was 132,35 mg/mL. The Optimum condition of protease enzyme were pH 7,0 and temperature 45 ⁰C with an activity value of 0,0463 U/mL. Protease activity could be inhibited by MnCl2 concentration of 0,01 - 0,03 M.Downloads
References
Baehaki, A., Suhartono, M.T., Palupi, N.S., and Nuhayati, T., Characterization of proteases from pathogenic bacteria Staphylococcus
aureus and Klebsiella sp. National Prosiding Seminar and Congress
PATPI, ISBN:979-99965-0-3, pp. 281–287, 2004.
Baehaki, A., Nurhayati, T., and Suhartono, M.T., Characteristics of Protease from Bacte-rial Pathogens Staphylococcus epidermidis, Bul-letin
of Fishery Product Technology, vol.8, no. 2, pp. 25–35 , 2005
Baehaki, A., Rinto, and Budiman, A., Isolation and Characterization of Protease from Bacterial Swamp Land Indralaya, J. Teknol. and Food Industry, vol. 22, no. 1, pp. 37–42,2011.
Beg, Q.K., and Gupta, R., Purification and Characterization of An Oxidationstable, Thiol-dependent Serine Alkaline Protease from Bacillus mojavensis, Enzyme and Microbial Tech-nology, vol. 32, no. 2, pp. 294–304, 2003
Dixon, E.C., and Webb, M.A, Enzymes, 3rd Edi-tion, Longman, Australia, 1979.
Falch, E.A., Industrial Enzymes Developments in Production and
Application, Biotech, vol. 9, pp. 643–658, 1991.
Kandolla, H., The Influence of CaCl2 on Production Protease Enzyme from Bacillus licheniformis HSA3-1a, Graduated Research, FMIPA, Hasanuddin University, Makassar, 2013.
Kuddus, M. and Ramteke, P.W., A Cold-Active Extracelullar Metalloprotease from Curto-bacterium luteum (MTCC 7529): Enzyme
Production and Characterization, J.Gen. Appl. Microbiol., vol. 54, pp. 385–392, 2008.
Moon, S.H. and Parulekar, S.J., Some Observation on Protease Producing in Continu-ous Suspention Cultures of Bacillus firmus, Biotech-Bioeng, vol.41, pp 43–54, 1993.
Natsir, H., Patong, A.R., Suhartono, M.T., and Ahmad, A., Production and Characterization of Chitinase Enzymes from Sulili Hot Spring in South
Sulawesi, Bacillus sp. HSA3-1a, Indo. J. Chem., vol. 10, no. 2, pp. 263–267, 2010.
Olajuyigbe, F.M., and Ajele, J.O., Some Properties of Extracellular
Protease from Bacillus licheniformis Lbbl-11 Isolated from “iru”, A Traditionally Fermented African Locust Bean Condiment, G. Journal of
Biotechnology & Biochemistry, vol. 3, no 1, pp. 42–46, 2008.
Oren, A., Halophilic microorganism and their environment, Kluwer Academic Publiser, pp. 143–162, 2003.
Poliana, J., and MacCabe, A.P., Industrial Enzymes; Structure, Function, and Applications, Dordrecht, Springer, 2007.
Richardson, T. and Hyslop, D.B., Enzyme, Mac Kerel Bekker, Inc.New
York, 1985.
Saono, S., and Basuki, T., The Amylolitic, Lipolytic and Proteolitic Activities of Yeast and Mycelial Molds from Ragi and Some Indonesia Traditional Frementated Foods, Annales Bogori-enses, vol. 4, pp. 207–219, 1978.
Sudarmadji, S., Haryono, B., and Suhardi., Analysis of Food and Agriculture, Gadjah Mada, Yogyakarta, 1989.
Sumardjo, D., Introduction Chemistry, Book Medical Publishers EGC, Jakarta, 2006.
Walter, H.E., Method with Haemoglobin, Cas-ein, and Azocoll as Substrate In, Bergmeyer, HU (ed), Methods of Enzymatic Analysis, Verlag
Chemie, Florida, 1984.
Whitaker, J.R., Principles of Enzymology for Food Sciences, Marcel Dekker Ltd, New York, 1972.
