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Novel insight into the secretory expression of recombinant enzymes in Escherichia coli

Paper ID Volume ID Publish Year Pages File Format Full-Text
34705 45040 2014 5 PDF Available
Title
Novel insight into the secretory expression of recombinant enzymes in Escherichia coli
Abstract

•Secretory expression of an extracellular enzyme CGTase in E. coli was investigated.•Overexpressed pre-proteins aggregated near inner side of E. coli inner membrane.•The rate of pre-protein synthesis and translocation should be balanced.

The secretory expression of recombinant enzymes in Escherichia coli has generally been a challenging task. In the present study, we investigated the expression of the extracellular enzyme cyclodextrin glycosyltransferase in E. coli. Our results indicated that when the overexpressed pre-proteins were not translocated across the inner membrane in a timely manner, they aggregated near the inner side of the E. coli inner membrane, resulting in the formation of insoluble inclusion bodies, which eventually blocked the pre-protein translocation channels and subsequently impeded further protein secretion. This mechanism suggests that for the efficient production of extracellular enzymes in E. coli, it is very important to maintain a balance between the rate of pre-protein synthesis and translocation, which can be achieved by altering the cultivation process. Our findings provide novel insight into the secretory expression of extracellular enzymes and may shed light on the further development of new strategies for extracellular protein production in E. coli.

Keywords
Secretory expression; Escherichia coli; Recombinant enzymes; Cyclodextrin glycosyltransferase
First Page Preview
Novel insight into the secretory expression of recombinant enzymes in Escherichia coli
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 4, April 2014, Pages 599–603
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering