scholarly journals A new potential secretion pathway for recombinant proteins in Bacillus subtilis

2015 ◽  
Vol 14 (1) ◽  
Author(s):  
Guangqiang Wang ◽  
Yongjun Xia ◽  
Zhennan Gu ◽  
Hao Zhang ◽  
Yong Q. Chen ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Recombinant Proteins ◽  
Secretion Pathway

scholarly journals The multifunctionality of expression systems in Bacillus subtilis: Emerging devices for the production of recombinant proteins

2021 ◽  
pp. 153537022110301
Author(s):  
Caio Coutinho de Souza ◽  
Jander Matos Guimarães ◽  
Soraya dos Santos Pereira ◽  
Luis André Morais Mariúba
Keyword(s):  
Bacillus Subtilis ◽  
Recombinant Proteins ◽  
Large Scale ◽  
Recombinant Expression ◽  
Academic Research ◽  
Future Research ◽  
Expression Systems ◽  
Bioactive Substances ◽  
Exogenous Dna ◽  
Chemical Inducers

Bacillus subtilis is a successful host for producing recombinant proteins. Its GRAS (generally recognized as safe) status and its remarkable innate ability to absorb and incorporate exogenous DNA into its genome make this organism an ideal platform for the heterologous expression of bioactive substances. The factors that corroborate its value can be attributed to the scientific knowledge obtained from decades of study regarding its biology that has fostered the development of several genetic engineering strategies, such as the use of different plasmids, engineering of constitutive or double promoters, chemical inducers, systems of self-inducing expression with or without a secretion system that uses a signal peptide, and so on. Tools that enrich the technological arsenal of this expression platform improve the efficiency and reduce the costs of production of proteins of biotechnological importance. Therefore, this review aims to highlight the major advances involving recombinant expression systems developed in B. subtilis, thus sustaining the generation of knowledge and its application in future research. It was verified that this bacterium is a model in constant demand and studies of the expression of recombinant proteins on a large scale are increasing in number. As such, it represents a powerful bacterial host for academic research and industrial purposes.

Expression Vectors for the Rapid Purification of Recombinant Proteins in Bacillus subtilis

2007 ◽  
Vol 55 (2) ◽  
pp. 89-93 ◽  
Author(s):  
Hoang Duc Nguyen ◽  
Trang Thi Phuong Phan ◽  
Wolfgang Schumann
Keyword(s):  
Bacillus Subtilis ◽  
Recombinant Proteins ◽  
Expression Vectors ◽  
Rapid Purification

scholarly journals Display of Recombinant Proteins on Bacillus subtilis Spores, Using a Coat-Associated Enzyme as the Carrier

2010 ◽  
Vol 76 (17) ◽  
pp. 5926-5933 ◽  
Author(s):  
Sébastien Potot ◽  
Cláudia R. Serra ◽  
Adriano O. Henriques ◽  
Ghislain Schyns
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Recombinant Proteins ◽  
Animal Feed ◽  
Active Form ◽  
Bioactive Molecules ◽  
Full Potential ◽  
Spore Surface ◽  
Outer Coat ◽  
Feed Enzymes

ABSTRACT The display of proteins such as feed enzymes at the surface of bacterial spore systems has a great potential use for animal feed. Feed enzymes increase the digestibility of nutrients, leading to greater efficiency in the manufacturing of animal products and minimizing the environmental impact of increased animal production. To deliver their full potential in the gut, feed enzymes must survive the harsh conditions of the feed preparation and the gastrointestinal tract. The well-documented resistance of spores to harsh environments, together with the ability to use proteins that compose the spore as carriers for the display of passenger proteins, suggests that spores could be used as innovative tools to improve the formulation of bioactive molecules. Although some successful examples have been reported, in which abundant structural proteins of the Bacillus subtilis spore outer-coat layer were used as carriers for the display of recombinant proteins, only one convincing example resulted in the display of functional enzymes. In addition, no examples are available about the use of an inner-coat protein for the display of an active passenger enzyme. In our study, we show that the inner-coat oxalate decarboxylase (OxdD) can expose an endogenous phytase, a commonly used feed enzyme for monogastric animals, in an active form at the spore surface. Importantly, despite the higher abundance of CotG outer-coat protein, an OxdD-Phy fusion was more represented at the spore surface. The potential of OxdD as a carrier protein is further documented through the spore display of a bioactive heterologous passenger, the tetrameric β-glucuronidase enzyme from Escherichia coli.

scholarly journals Analysis and application of Bacillus subtilis sortases to anchor recombinant proteins on the cell wall

AMB Express ◽  
2011 ◽  
Vol 1 (1) ◽  
pp. 22 ◽  
Author(s):  
Hoang Nguyen ◽  
Trang Phan ◽  
Wolfgang Schumann
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Recombinant Proteins

scholarly journals Deleting multiple lytic genes enhances biomass yield and production of recombinant proteins by Bacillus subtilis

2014 ◽  
Vol 13 (1) ◽  
Author(s):  
Yi Wang ◽  
Zhenmin Chen ◽  
Ruili Zhao ◽  
Tingting Jin ◽  
Xiaoming Zhang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Recombinant Proteins ◽  
Biomass Yield ◽  
Lytic Genes

scholarly journals Improving the production of AHL lactonase AiiO-AIO6 from Ochrobactrum sp. M231 in intracellular protease-deficient Bacillus subtilis

2020 ◽  
Author(s):  
Rui Xia ◽  
Yalin Yang ◽  
Xingliang Pan ◽  
Chenchen Gao ◽  
Yuanyuan Yao ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Positive Impact ◽  
Cell Communication ◽  
Quorum Quenching ◽  
Catalytic Triad ◽  
Heterologous Proteins ◽  
Extracellular Production ◽  
Secretion Pathway ◽  
Protease Deficient ◽  
Encoding Genes

Abstract Quorum quenching (QQ) blocks bacterial cell-to-cell communication (i.e., quorum sensing), and is a promising antipathogenic strategy to control bacterial infection via inhibition of virulence factor expression and biofilm formation. QQ enzyme AiiO-AIO6 from Ochrobactrum sp. M231 has several excellent properties and shows biotherapeutic potential against important bacterial pathogens of aquatic species. AiiO-AIO6 can be secretory expressed in Bacillus subtilis via a non-classical secretion pathway. To improve AiiO-AIO6 production, four intracellular protease-deletion mutants of B. subtilis 1A751 were constructed by individually knocking out the intracellular protease-encoding genes (tepA, ymfH, yrrN and ywpE). The AiiO-AIO6 expression plasmid pWB-AIO6BS was transformed into the B. subtilis 1A751 and its four intracellular protease-deletion derivatives. Results showed that all recombinant intracellular protease-deletion derivatives (BSΔtepA, BSΔymfH, BSΔyrrN and BSΔywpE) had a positive impact on AiiO-AIO6 production. The highest amount of AiiO-AIO6 extracellular production of BSΔywpE in shake flask reached 3530 U/mL, which was about 62% higher than that of the wild-type strain. Furthermore, LC-MS/MS analysis of the degrading products of 3-oxo-C8-HSL by purification of AiiO-AIO6 indicated that AiiO-AIO6 was an AHL-lactonase which hydrolyzes the lactone ring of AHLs. Phylogenetic analysis showed that AiiO-AIO6 was classified as a member of the α/β hydrolase family with a conserved “nucleophile-acid-histidine” catalytic triad. In summary, this study showed that intracellular proteases were responsible for the reduced yields of heterologous proteins and provided an efficient strategy to enhance the extracellular production of AHL lactonase AiiO-AIO6.

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