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Molecular cloning, purification and characterization of thermostable <img src='/image/spc_char/beta.gif' border=0>-1,3-1,4 glucanase from <i>Bacillus subtilis </i>A8-8

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Title Molecular cloning, purification and characterization of thermostable -1,3-1,4 glucanase from Bacillus subtilis A8-8
 
Creator Jung, Youn-Ju
Lee, Yong-Seok
Park, In-Hye
Chandra, M Subhosh
Kim, Keun-Ki
Choi, Yong-Lark
 
Subject Bacillus subtilis
Glucanase
Cellulose-binding domain
Catalytic domain
Purification
 
Description 203-210
A gene encoding a -1,3-1,4-glucanase (CelA)
belonging to family
5 of glycoside hydrolases was cloned and sequenced from the Bacillus
subtilis A8-8.
The open-reading-frame of celA comprised 1499 base pairs and the enzyme was composed of 500 amino
acids with a molecular mass of 55 kDa. The recombinant -1,3-1,4 glucanase was purified by GST-fusion purification system. The
pH and temperature optima of the enzyme were 8.0 and 60oC,
respectively. The enzyme was stable within pH 6.0-9.0. It was stable up to 60oC
and retained 30% of
its original activity at 70oC for 60 min. It hydrolyzed lichenan, CMC, xylan, laminarin, avicel and pNPC, but was inactive towards
cellobiose. The enzyme activity was markedly activated by Co2+ and
Mn2+, but was strongly inactivated by Fe3+. The truncated
gene, devoid of cellulose-binding domain (CBD) showed 60% of activity and bound
to avicel.
 
Date 2010-08-23T06:29:57Z
2010-08-23T06:29:57Z
2010-08
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/10119
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol.47(4) [August 2010]