Characterization of chondroitinase 1816 from Microbulbifer sp. ALW1
作者单位：College of Food and Biological Engineering
会议名称：《中国生物化学与分子生物学会第十二届全国会员代表大会暨2018年全国学术会议》
会议日期：2018年
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术]
关 键 词：Chondroitinase Enzymatic properties Enzymatic hydrolysate
摘 要：The gene of chondroitinase 1816(ChSase1816) was overexpressed and purified from Escherichia coli BL21(DE3) with a molecular mass of 86 *** the chondroitin sulfate B(CS-B) as the substrate,the Km and Vmax values of ChSase1816 towards CS-B was 7.85 μg/mL and 1.21 U/*** optimum reaction temperature and pH for ChSase1816 were 30℃ and 8.0,*** ChSase1816 activity was stable at 30°C,but not stable at 50°C and 60°***,ChSase1816 retained more than 60% of its maximum activity at a broad pH range of pH 4.0 and *** the metal ions detected had inhibitory effects on the *** result of Circular dichroism(CD) indicated the enzyme contained many antiparallel structure and random *** antioxidant activity assay showed that hydroxyl radical scavenging activity of chondroitin enzymatic hydrolysates was higher than chondroitin sulfate.