Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in Bacillus

Abstract:

Bacillus subtilis is a well-established cellular factory for proteins and fine chemicals. In particular, the direct secretion of proteinaceous products into the growth medium greatly facilitates their downstream processing, which is an important advantage of B. subtilis over other biotechnological production hosts, such as Escherichia coli. The application spectrum of B. subtilis is, however, often confined to proteins from Bacillus or closely related species. One of the major reasons for this (current) limitation is the inefficient formation of disulfide bonds, which are found in many, especially eukaryotic, proteins. Future exploitation of B. subtilis to fulfill the ever-growing demand for pharmaceutical and other high-value proteins will therefore depend on overcoming this particular hurdle. Recently, promising advances in this area have been achieved, which focus attention on the need to modulate the cellular levels and activity of thiol-disulfide oxidoreductases (TDORs). These TDORs are enzymes that control the cleavage or formation of disulfide bonds. This review will discuss readily applicable approaches for TDOR modulation and aims to provide leads for further improvement of the Bacillus cell factory for production of disulfide bond-containing proteins.

SEEK ID: https://fairdomhub.org/publications/76

PubMed ID: 19727703

Projects: BaCell-SysMO

Publication type: Not specified

Journal: Appl. Microbiol. Biotechnol.

Citation:

Date Published: 11th Jun 2009

Registered Mode: Not specified

Authors: Thijs R H M Kouwen,

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Created: 20th Aug 2010 at 13:59

Last updated: 8th Dec 2022 at 17:26

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