Partial biochemical characterization of crude extract extracellular chitinase enzyme from Bacillus subtilis B 298

11th Joint Conference on Chemistry in Conjunction with the 4th Regional Biomaterials Scientific Meeting

材料科学;化学;生物科学

Lestari, P.^1 ; Prihatiningsih, N.^2 ; Djatmiko, H.A.^2

Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Jenderal Soedirman, Purwokerto, Indonesia^1

Department of Agrotechnology, Faculty of Agricultural, University of Jenderal Soedirman, Purwokerto, Indonesia^2

关键词: Bacillus Subtilis;    Biochemical characterization;    Chitinase activities;    Divalent cation;    Enzyme production;    Extracellular chitinases;    Optimum activity;    Production curve;   

Others  :  https://iopscience.iop.org/article/10.1088/1757-899X/172/1/012041/pdf
DOI  :  10.1088/1757-899X/172/1/012041

来源: IOP

【 摘 要 】

Extraction and characterization of extracellular chitinase from Bacillus subtilis B 298 have been done. Growth curve determination of B. subtilis B 298, production curve determination of crude extract chitinase from B. subtilis B 298, and partial biochemical characterization of crude extract chitinase have been achieved in this study. Optimum growth of B. subtilis B 298 was achieved at logarithmic phase within 9 hours incubation time, so it was used as inoculum for enzyme production. According to production curve of the enzyme, it was known that incubation time which gave the highest chitinase activity of 15 hours with activity of 6.937 U/mL respectively. Effect of various temperatures on chitinase activity showed that optimum activity was achieved at 40°C with an activity of 5.764 U/mL respectively. Meanwhile, the optimum pH for chitinase activity was achieved at pH of 5.0 with an activity of 6.813 U/mL respectively. This enzyme was then classified as metalloenzyme due to the decline of the activity by EDTA addition. All divalent cations tested acted as inhibitors.