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Title 

Expression and activation of an esterase from Pseudomonas aeruginosa 1001 in Escherichia coli

Authors 

Je Hyuk LeeSang Ki RheeChul Ho Kim

Publisher 

Elsevier

Issue Date 

2004

Citation 

Enzyme and Microbial Technology, vol. 35, no. 6, pp. 563-567

Keywords 

esterasemaltose binding proteinpseudomonas aeruginosaescherichia colienzyme activationexpression vectorgene overexpressionprotein expression

Abstract 

An expression vector was constructed to overproduce a maltose binding protein (MBP)-esterase fusion protein in Escherichia coli. Soluble fusion protein was separated by centrifugation after cell disruption. The fusion protein was partially purified with amylose resin. The higher concentration of fusion protein (above 2 mg/ml) did not show any activity but about 0.3 mg/ml of fusion protein had the highest activity (142 U/ml). It is due to the difficulty of contact between substrate and active site of enzyme in compact form at high concentration. The fusion protein over-expressed could not be separated into MBP and esterase by the action of protease 'Factor Xa'. The esterase could be cleaved from MBP fusion protein by the treatment of SDS with the Factor Xa, and the resulting esterase activity was increased to 34% after cleavage.

ISSN 

0141-0229

Link 

http://dx.doi.org/10.1016/j.enzmictec.2004.08.029

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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