Innovative Research/Bacillus Polymyxa Neutral Protease Partially Purified/IRWBE673/5gm

摘要： 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°C 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°C, respectively, where ACTase showed chitosan degrading activity (87%), which was enhanced by 15% in the presence of calcium ions (8mM). The ACTase produced from B.cereus GU-02 was partially purified from the culture supernatant, and its enzymatic activity was kinetically characterized. The Vmax and Km were estimated with a chitosan (degree of deacetylation, DD 92% as substrate) as 0.038U/min/μg protein and 0.327μM, 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. 展开 我们已与文献出版商建立了直接购买合作。 你可以通过身份认证进行实名认证，认证成功后本次下载的费用将由您所在的图书馆支付 您可以直接购买此文献，1~5分钟即可下载全文，部分资源由于网络原因可能需要更长时间，请您耐心等待哦~