食品与发酵工业2012，Vol.38Issue(7)：114-119,6.
黏质沙雷氏菌胞外几丁质酶的纯化及特性
Purification and Characterization of Extracellular Chitinase from Serratia marcescens
施腾鑫 1黄秀菁 1刘嘉 2贺淹才2
作者信息
- 1. 福建福大百特科技发展有限公司酶高效表达国家工程实验室,福建福州350000
- 2. 华侨大学工业生物技术研究所,福建泉州362021
- 折叠
摘要
Abstract
An extracellular chitinase and a chitin-binding protein （CBP21） were isolated from the culture of Serratia marcescens and purified to electrophoretic homogeneity by ordinal procedures containing ammonium sulfate precipitation, DEAE-Sepharose and Phenyl-Sepharose chromatography. Their relative molecular masses were estimated to be respectively about 58kD and 21kD by SDS-PAGE. CBP21 had great synergistic effect with the chitinase on chitin hydrolysis. The optimum temperature and pH for the enzyme activity were 50℃ and 6.5 respectively. The enzyme activity was stable under 55℃ and in the pH range of 4.5 - 8.0. Michaelis constants of the enzyme were Km 0.22 mg/ mL and Vm 1.26 ixmol/（min·mg） respectively. The activity was enhanced by K＋, Sn2＋ and Mn2＋ and was strong- ly inhibited by Pb2＋ , Hg2＋ and Cu2＋. EDTA and 2-mercaptoethanol （2-ME） enhanced the activity by 65% and 105% respectively. H2O2 strongly inhibited chitinase activity, which indicated that hydrosulfide group was the possi- ble essential residue for enzyme activity.关键词
黏质沙雷氏菌/几丁质酶/纯化/特性Key words
Serratia marcescens/chitinase/purification/characterization分类
生物科学引用本文复制引用
施腾鑫,黄秀菁,刘嘉,贺淹才..黏质沙雷氏菌胞外几丁质酶的纯化及特性[J].食品与发酵工业,2012,38(7):114-119,6.
