Characterization of an alkalophilic extracellular chitosanase from Bacillus cereus GU-02(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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An alkalophilic extracellular chitosanase (ACTase) was characterized from the culture supernatant of Bacillus cereus GU-02. Kinetic properties of ACTase produced from B. cereus GU-02 after cultivation in anaerobic condition, alkaline medium (pH 10) at 37℃ for 3 days were investigated. ACTase was found to be stable in alkaline pH range from 8 to 10. Interestingly, optimum pH and temperature were estimated to be 10 and 37℃, respectively, where ACTase showed chitosan degrading activity (87%), which was enhanced by 15% in the presence of calcium ions (8 mM). The ACTase produced from B. cereus GU-02 was partially purified from the culture supernatant, and its enzymatic activity was kinetically characterized. The V_<max> and K_m were estimated with a chitosan (degree of deacetylation, DD 92% as substrate) as 0.038 U/min/μg protein and 0.327 μM, respectively. A combination of the TLC and MALDI-TOF MS results showed that the chitosan oligosaccharides obtained from the hydrolysis of high molecular weight chitosan (HMWC) by ACTase of the B. cereus GU-2 comprise oligomers with degree of polymerization (DP) mainly from dimers to pentamers. High production of ACTase and chitooligosaccharides may be useful for various industrial and biological applications.
著者
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Park Jae
Department of Advanced Materials Science and Engineering, Sungkyunkwan University, Suwon, Kyunggi-do 440-746, South Korea
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Park Jae
Department of Life Science, College of Bionano, Gachon University
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Goo Bon
Department of Pharmaceutical Science, Gachon University
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- Characterization of an alkalophilic extracellular chitosanase from Bacillus cereus GU-02(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)