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IJBB Vol.47(4) [August 2010] >


Title: Molecular cloning, purification and characterization of thermostable -1,3-1,4 glucanase from Bacillus subtilis A8-8
Authors: Jung, Youn-Ju
Lee, Yong-Seok
Park, In-Hye
Chandra, M Subhosh
Kim, Keun-Ki
Choi, Yong-Lark
Keywords: Bacillus subtilis
Glucanase
Cellulose-binding domain
Catalytic domain
Purification
Issue Date: Aug-2010
Publisher: CSIR
Abstract: 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.
Page(s): 203-210
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Source:IJBB Vol.47(4) [August 2010]

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