Heterologous expression and characterization of detergent stable endoglucanase EG5B from Paenibacillus sp. IHB B 3084
The endoglucanase gene EG5B of 1611 bp with a predicted molecular weight of 58.6 kDa
from Paenibacillus sp. IHB B 3084 was cloned and expressed in Escherichia coli BL21
(DE3). The analysis of deduced amino acid sequence revealed a modular structure of the
endoglucanase EG5B with an N-terminal catalytic domain of glycosyl hydrolase family 5 and
a C-terminal carbohydrate-binding module of family 3. The purified enzyme showed high
hydrolytic activity on carboxymethylcellulose, low activity on p-nitrophenyl β-d-cellobioside …
from Paenibacillus sp. IHB B 3084 was cloned and expressed in Escherichia coli BL21
(DE3). The analysis of deduced amino acid sequence revealed a modular structure of the
endoglucanase EG5B with an N-terminal catalytic domain of glycosyl hydrolase family 5 and
a C-terminal carbohydrate-binding module of family 3. The purified enzyme showed high
hydrolytic activity on carboxymethylcellulose, low activity on p-nitrophenyl β-d-cellobioside …
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