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Title

New approaches to achieve high level enzyme production in Streptomyces lividans

AuthorsSevillano, Laura ; Vijgenboom, Erik; Wezel, Gilles P. van; Díaz, Margarita ; Santamaría, Ramón I.
KeywordsStreptomyces
Protein production
Xylanase
Amylase
Laccase
Vector optimization
Issue Date2016
PublisherBioMed Central
CitationMicrobial Cell Factories 15: 28 (2016)
Abstract[Background]: Actinomycetes are saprophytic soil bacteria, and a rich source of industrial enzymes. While some of these enzymes can be produced using well-characterized production platforms such as Escherichia coli or Bacillus subtilis, Streptomyces lividans may be the preferred host for proper folding and efficient secretion of active enzymes. A combination of promoters, signal peptides and hosts were tested in order to obtain the best protein expression in this actinomycete. The xylanase, Xys1, from S. halstedii, the α-amylase, Amy, from S. griseus and the small laccase, SLAC, from S. coelicolor were used as reporters. [Results]: The promoters xysAp from S. halstedii JM8 and pstSp from S. lividans were the most efficient among those tested. An improvement of 17 % was obtained in xylanase activity when the signal peptide of the α-amylase protein (Amy) of S. griseus IMRU3570 was used to direct its secretion. Enhanced expression of SsgA, a protein that plays a role in processes that require cell-wall remodelling, resulted in a improvement of 40 and 70 % of xylanase and amylase production, respectively. Deletion of genes SLI7232 and SLI4452 encoding putative repressors of xysAp provided improvement of production up to 70 % in the SLI7232 deletion strain. However, full derepression of this promoter activity was not obtained under the conditions assayed. [Conclusions]: Streptomyces lividans is a frequently used platform for industrial enzyme production and a rational strain-development approach delivered significant improvement of protein production by this host.
DescriptionThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://​creativecommons.​org/​licenses/​by/​4.​0/​).
Publisher version (URL)http://dx.doi.org/10.1186/s12934-016-0425-7
URIhttp://hdl.handle.net/10261/130711
DOI10.1186/s12934-016-0425-7
ISSN1475-2859
Appears in Collections:(IBFG) Artículos
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