当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > A novel cold-adapted and glucose-tolerant GH1 β-glucosidase from Exiguobacterium antarcticum B7.

A novel cold-adapted and glucose-tolerant GH1 β-glucosidase from Exiguobacterium antarcticum B7.

Abstract：

:A novel GH1 β-glucosidase (EaBgl1A) from a bacterium isolated from Antarctica soil samples was recombinantly overexpressed in Escherichia coli cells and characterized. The enzyme showed unusual pH dependence with maximum activity at neutral pH and retention of high catalytic activity in the pH range 6 to 9, indicating a catalytic machinery compatible with alkaline conditions. EaBgl1A is also a cold-adapted enzyme, exhibiting activity in the temperature range from 10 to 40°C with optimal activity at 30°C, which allows its application in industrial processes using low temperatures. Kinetic characterization revealed an enzymatic turnover (Kcat) of 6.92s(-1) (cellobiose) and 32.98s(-1) (pNPG) and a high tolerance for product inhibition, which is an extremely desirable feature for biotechnological purposes. Interestingly, the enzyme was stimulated by up to 200 mM glucose, whereas the commercial cocktails tested were found fully inhibited at this concentration. These properties indicate EaBgl1A as a promising biocatalyst for biotechnological applications where low temperatures are required.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Crespim E,Zanphorlin LM,de Souza FH,Diogo JA,Gazolla AC,Machado CB,Figueiredo F,Sousa AS,Nóbrega F,Pellizari VH,Murakami MT,Ruller R

doi

10.1016/j.ijbiomac.2015.09.018

subject

Has Abstract

pub_date

2016-01-01 00:00:00

pages

375-80

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(15)00633-9

journal_volume

82

pub_type

杂志文章

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