内生真菌β-D-葡萄糖醛酸苷酶固定化及其性质研究  

Immobilization and properties of a high-selectivity β-D-glucuronidase from endophytic fungus Chaetomium globosum S108

作　　者：闫宜江 肖依文[1] 汪涯[1] 吴文婷[1] 常军[1] 何巧璇 朱笃[1,2] 

机构地区：[1]江西科技师范大学生命科学学院,江西省生物加工过程重点实验室,江西南昌330013 [2]江西师范大学生命科学学院,江西省亚热带植物资源保护与利用重点实验室,江西南昌330022 [3]中国成达工程有限公司,四川成都610041

出　　处：《食品与发酵工业》2017年第7期49-54,共6页Food and Fermentation Industries

基　　金：国家自然科学基金项目(31260137);“赣鄱英才555工程”领军人才计划项目;江西科技师范大学自然科学科研计划项目(2016XJZD001)资助

摘　　要：以海藻酸钠为载体、戊二醛为交联剂,对内生真菌Chaetomium globosum S108的高选择性β-D-葡萄糖醛酸苷酶的固定化及部分特性进行了研究。结果表明:β-D-葡萄糖醛酸苷酶的最佳固定化条件为海藻酸钠1.5%、戊二醛1.5%、添加酶量3 500 U、Ca Cl2浓度2%,交联时间30 min。β-D-葡萄糖醛酸苷酶固定化后,其最适温度提高5℃,最佳pH值由6.0~6.8拓展为5.2~7.6,热稳定性和pH稳定性明显改善;米氏常数(Km)明显增大,而最大反应初速度(Vmax)明显减小。固定化酶重复操作15次,其相对酶活仍保持71%。A high-selectivity β-D-glucuronidase from Endophytic Fungus Chaetomium globosum S108 was immo- bilized into matrix with sodium alginate as embedding material and glutaraldehyde as crosslinking agent. The optimal immobilized conditions were achieved with 1.5% sodium alginate, 1.5% glutaraldehyde, 2% CaC12 and 3 500 U of enzyme load of per milliliter matrix for 30 min. In addition, some immobilized enzymology properties were studied. Compared with free enzyme, the optimum temperature and pH of immobilized enzyme were higher than those of free form, and temperature stability and pH stability of immobilized enzyme were enhanced obviously. After immobilization of β-D-glucuronidase, the Michaelis decreased respectively. Immobilized consecutive 15 cycles. constant （Km） was increased, and the maximum reaction velocity （Vmax） was β-D-glucuronicdase enzyme activity still retained 71% of its initial activity after.

关 键 词：海藻酸钠 β-D-葡萄糖醛酸苷酶 甘草酸 固定化 内生真菌 

分 类 号：Q814.2[生物学—生物工程]