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

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About: Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in Bacillus Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in Bacillus
Creator	Kouwen, Thijs Maarten Van Dijl, Jan
topic	covid:d9903d349512b4dbd6e05c03ac680a0cb1ac1d0b#this
source	PMC
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.
has issue date	2009-09-03(xsd:dateTime)
bibo:doi	10.1007/s00253-009-2212-4
bibo:pmid	19727703
has license	no-cc
sha1sum (hex)	d9903d349512b4dbd6e05c03ac680a0cb1ac1d0b
schema:url	https://doi.org/10.1007/s00253-009-2212-4
resource representing a document's title	Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in Bacillus
has PubMed Central identifier	PMC2765640
has PubMed identifier	19727703
schema:publication	Appl Microbiol Biotechnol
resource representing a document's body	covid:d9903d349512b4dbd6e05c03ac680a0cb1ac1d0b#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/d9903d349512b4dbd6e05c03ac680a0cb1ac1d0b
is schema:about of	named entity 'improvement' named entity 'proteins' named entity 'disulfide' named entity 'species' named entity 'proteins' named entity 'PROTEINACEOUS' named entity 'ADVANTAGE' named entity 'HAVE' named entity 'FULFILL' named entity 'oxidoreductases' named entity 'focus' named entity 'Future' named entity 'B. subtilis' named entity 'production' named entity 'hurdle' named entity 'cell' named entity 'eukaryotic' named entity 'area' named entity 'cellular' named entity 'hosts' named entity 'oxidoreductases' named entity 'production' named entity 'B. subtilis' named entity 'fine chemicals' named entity 'Escherichia coli' named entity 'eukaryotic' named entity 'disulfide bonds' named entity 'growth medium' named entity 'thiol' named entity 'disulfide' named entity 'oxidoreductases' named entity 'disulfide' named entity 'oxidoreductases' named entity 'cell surface' named entity 'DsbA' named entity 'genetic modification' named entity 'protein production' named entity 'E. coli' named entity 'heterologous' named entity 'B. subtilis' named entity 'thiol' named entity 'protease' named entity 'protein' named entity 'eukaryotic' named entity 'growth medium' named entity 'protein' named entity 'secretion' named entity 'B. subtilis' named entity 'oxidases' named entity 'production of proteins' named entity 'E. coli' named entity 'heterologous' named entity 'B. subtilis' named entity 'B. subtilis' named entity 'selective pressure' named entity 'DsbB' named entity 'Hederstedt' named entity 'isomerize' named entity 'B. subtilis' named entity 'disulfide bonds' named entity 'B. subtilis' named entity 'microorganisms' named entity 'disulfide bond formation' named entity 'Incubation' named entity 'disulfide' named entity 'oxidases' named entity 'B. subtilis' named entity 'oxidized form' named entity 'cytoplasmic' named entity 'E. coli' named entity 'S. aureus' named entity 'conformation' named entity 'bioinformatic' named entity 'BdbC' named entity 'protein secretion' named entity 'isomerization' named entity 'disulfide bonds' named entity 'B. subtilis'

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