从 Aspergillus nidulans 突变株 USDB 1183 中分离和鉴定β-葡萄糖苷酶。

Isolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183.

机构信息

Department of Botany, Faculty of Science, National University of Singapore, 10 Kent Ridge Crescent, 0511, Singapore, Singapore.

出版信息

World J Microbiol Biotechnol. 1993 Sep;9(5):555-8. doi: 10.1007/BF00386292.

DOI:10.1007/BF00386292

PMID:24420198

Abstract

Two extracellular β-glucosidases (cellobiase, EC 3.2.1.21), I and II, from Aspergillus nidulans USDB 1183 were purified to homogeneity with molecular weights of 240,000 and 78,000, respectively. Both hydrolysed laminaribiose, β-gentiobiose, cellobiose, p-nitrophenyl-β-L-glucoside, phenyl-β-L-glucoside, o-nitrophenyl-β-L-glucoside, salicin and methyl-β-L-glucoside but not α-linked disaccharides. Both were competitively inhibited by glucose and non-competitively (mixed) inhibited by glucono-1,5-lactone. β-Glucosidase I was more susceptible to inhibition by Ag(+) and less inhibited by Fe(2+) and Fe(3+) than β-glucosidase II.

摘要

两株来自曲霉菌（Aspergillus nidulans USDB 1183）的细胞外β-葡萄糖苷酶（纤维素酶，EC 3.2.1.21）I 和 II 被纯化为均一性，分子量分别为 240000 和 78000。两者均可水解纤维二糖、β-龙胆二糖、纤维二糖、对硝基苯-β-L-葡萄糖苷、苯-β-L-葡萄糖苷、邻硝基苯-β-L-葡萄糖苷、水杨苷和甲基-β-L-葡萄糖苷，但不能水解α-连接的二糖。两者均被葡萄糖竞争性抑制，而被葡萄糖酸-1,5-内酯非竞争性（混合）抑制。β-葡萄糖苷酶 I 比β-葡萄糖苷酶 II 更易受 Ag(+)抑制，而受 Fe(2+)和 Fe(3+)抑制较小。