Paavilainen S, Hellman J, Korpela T
Department of Biochemistry, University of Turku, Finland.
Appl Environ Microbiol. 1993 Mar;59(3):927-32. doi: 10.1128/aem.59.3.927-932.1993.
An intracellular beta-glucosidase was purified from cell extracts of Bacillus circulans subsp. alkalophilus by NAD affinity and high-performance anion-exchange chromatographies. The enzyme was active against a wide range of aryl-beta-glucosides and beta-linked disaccharides. The structural gene for beta-glucosidase was cloned in Escherichia coli. The beta-glucosidase gene consisted of an open reading frame of 1,350 bp encoding a protein of 450 amino acids with a calculated M(r) of 51,303. The enzyme exhibited from 45 to 66% identity with five bacterial beta-glucosidases.
通过NAD亲和色谱和高效阴离子交换色谱从嗜碱环状芽孢杆菌亚种的细胞提取物中纯化出一种细胞内β-葡萄糖苷酶。该酶对多种芳基-β-葡萄糖苷和β-连接的二糖具有活性。β-葡萄糖苷酶的结构基因被克隆到大肠杆菌中。β-葡萄糖苷酶基因由一个1350 bp的开放阅读框组成，编码一个450个氨基酸的蛋白质，计算分子量为51303。该酶与五种细菌β-葡萄糖苷酶的同源性为45%至66%。
