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Heterologous expression and characterization of detergent stableendoglucanase EG5B from Paenibacillus sp. IHB B 3084

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Title Heterologous expression and characterization of detergent stableendoglucanase EG5B from Paenibacillus sp. IHB B 3084
 
Creator Hena Dhar
Ramesh Chand Kasana
Arvind Gulati
 
Subject Paenibacillus sp., Endoglucanase, Recombinant, Expression, Detergent stable
 
Description Not Available
tThe endoglucanase gene EG5B of 1611 bp with a predicted molecular weight of 58.6 kDa from Paenibacillussp. IHB B 3084 was cloned and expressed in Escherichia coli BL21(DE3). The analysis of deduced amino acidsequence revealed a modular structure of the endoglucanase EG5B with an N-terminal catalytic domainof glycosyl hydrolase family 5 and a C-terminal carbohydrate-binding module of family 3. The purifiedenzyme showed high hydrolytic activity on carboxymethylcellulose, low activity on p-nitrophenyl -d-cellobioside, avicel and filter paper, and no activity on microcrystalline cellulose, p-nitrophenyl -d-glucoside, cellobiose and salicin as substrates. The enzyme was mild-alkaline active with optimum activity at pH 7–8 and stable over broad pH range. The temperature optimum was at 50◦C with >50%activity over 30–60◦C. The enzyme stability with >63% residual activity towards non-ionic and anionic surfactants and commercial detergents suggested its compatibility as an additive to detergents.
Not Available
 
Date 2019-04-24T10:55:50Z
2019-04-24T10:55:50Z
2015-06-20
 
Type Research Paper
 
Identifier 6
Not Available
http://krishi.icar.gov.in/jspui/handle/123456789/18868
 
Language English
 
Relation Not Available;
 
Publisher Elsevier