Heterologous expression and purification of plantaricin NC8, a two-peptide bacteriocin against Salmonella spp. from Lactobacillus plantarum ZJ316

2016 ◽  
Vol 127 ◽  
pp. 28-34 ◽  
Author(s):  
Han Jiang ◽  
Ping Li ◽  
Qing Gu
Keyword(s):  
Heterologous Expression ◽  
Lactobacillus Plantarum ◽  
Expression And Purification ◽  
Salmonella Spp ◽  
Plantaricin Nc8 ◽  
Lactobacillus Plantarum Zj316

scholarly journals CONSTRUCTION, EXPRESSION AND PURIFICATION OF RECOMBINANT PRE-MATURE PEPTIDE OF PLANTARICIN F FROM Lactobacillus plantarum S34 IN Escherichia coli

2015 ◽  
Vol 16 (1) ◽  
pp. 31
Author(s):  
Kusdianawati Kusdianawati ◽  
Apon Zaenal Mustopa ◽  
Suharsono Suharsono ◽  
Bugi Ratno Budiarto ◽  
Fatimah Fatimah ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lactobacillus Plantarum ◽  
Proteolytic Enzymes ◽  
Leader Peptide ◽  
Human Consumption ◽  
Mature Peptide ◽  
Expression And Purification ◽  
Food Preservative ◽  
E Coli ◽  
Sds Page

Plantaricin is one of bacteriocins that have the potential to be used as food preservative. Plantaricin is safe for human consumption because it can be easily degraded by proteolytic enzymes. The objective of this study was to express and purify recombinant pre-mature peptide of plantaricin F from <em>Lactobacillus plantarum</em> S34 in <em>Escherichia coli</em>. Plantaricin gene-specific primer was used to obtain pln F structural gene amplicon from L. <em>plantarum</em> S34. This amplicon was cloned in pET32a vector and expressed in E. coli BL21 (DE3) pLysS. Pre-mature plantaricin F peptide was expressed as Histagged-fusion protein and separated by Co2+-chelating affinity chromatography. L. <em>plantarum</em> S34-derived pre-mature plantaricin F peptide fused with thioredoxin-(His)6tag had successfully been expressed in E. <em>coli</em> BL21 (DE3) pLysS using pET32a as an expression vector. The fused recombinant pln F as pre-mature state expressed had a molecular mass of +24 kDa, meanwhile the fused recombinant that contained only the leader peptide of pln F appeared as +20 kDa based on SDS-PAGE separations. The optimal production of fused recombinant pln F as soluble fraction was obtained when culture condition was added with 0.5 mM of IPTG and incubated at 22°C for 5 hours (OD~1). Furthermore, the expression of fused recombinant pln F as its pre-mature peptide pointed out that the pln F’s leader peptide could be proteolytically cleaved by a system in heterologous cells. Overall, heterologous pln F production as pre-mature peptide fused with thioredoxin-(His)6tag had been well established. From this research, we expect plantaricin F can be expressed and purified in E. coli.

Heterologous Expression and Purification of the Serotonin Type 4 Receptor from Transgenic Mouse Retina†

Biochemistry ◽  
2008 ◽  
Vol 47 (50) ◽  
pp. 13296-13307 ◽  
Author(s):  
David Salom ◽  
Nan Wu ◽  
Wenyu Sun ◽  
Zhiqian Dong ◽  
Krzysztof Palczewski ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Transgenic Mouse ◽  
Mouse Retina ◽  
Expression And Purification

Lactobacillus plantarum ZJ316 improves the quality of Stachys sieboldii Miq. pickle by inhibiting harmful bacteria growth and degrading nitrite, promoting the gut microbiota health in vitro

2022 ◽  
Author(s):  
Shu Ting Hang ◽  
Ling zhou Zeng ◽  
Jia run Han ◽  
Zhong qin Zhang ◽  
Qingqing Zhou ◽  
...  
Keyword(s):  
Quality Control ◽  
Lactic Acid ◽  
Lactobacillus Plantarum ◽  
Microbial Contamination ◽  
Nitrite Accumulation ◽  
Bacteria Growth ◽  
Lactobacillus Plantarum Zj316 ◽  
Stachys Sieboldii

Microbial contamination and nitrite accumulation are two major concerns on the quality control of fermented vegetables. In the present study, a lactic acid bacteria strain Lactobacillus plantarum ZJ316 (ZJ316) was...

scholarly journals Heterologous Expression and Purification Systems for Structural Proteomics of Mammalian Membrane Proteins

2002 ◽  
Vol 3 (6) ◽  
pp. 511-517 ◽  
Author(s):  
Isabelle Mus-Veteau
Keyword(s):  
Membrane Proteins ◽  
Heterologous Expression ◽  
Large Scale ◽  
Structural Information ◽  
Structural Data ◽  
Structural Proteomics ◽  
Scale Production ◽  
Expression And Purification ◽  
Large Scale Production ◽  
Heterologous Expression Systems

Membrane proteins (MPs) are responsible for the interface between the exterior and the interior of the cell. These proteins are implicated in numerous diseases, such as cancer, cystic fibrosis, epilepsy, hyperinsulinism, heart failure, hypertension and Alzheimer's disease. However, studies on these disorders are hampered by a lack of structural information about the proteins involved. Structural analysis requires large quantities of pure and active proteins. The majority of medically and pharmaceutically relevant MPs are present in tissues at very low concentration, which makes heterologous expression in large-scale production-adapted cells a prerequisite for structural studies. Obtaining mammalian MP structural data depends on the development of methods that allow the production of large quantities of MPs. This review focuses on the different heterologous expression systems, and the purification strategies, used to produce large amounts of pure mammalian MPs for structural proteomics.

Heterologous Expression of Oxalate Decarboxylase in Lactobacillus plantarum NC8

2008 ◽  
Vol 58 (2) ◽  
pp. 117-121 ◽  
Author(s):  
Anbazhagan Kolandaswamy ◽  
Leema George ◽  
Selvam Sadasivam
Keyword(s):  
Heterologous Expression ◽  
Lactobacillus Plantarum ◽  
Oxalate Decarboxylase

scholarly journals An Efficient Strategy for Heterologous Expression and Purification of Active Peptide Hainantoxin-IV

PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0117099 ◽  
Author(s):  
Hui Zhang ◽  
Peng-Fei Huang ◽  
Er Meng ◽  
Wen-Ying Li ◽  
Lu Zhou ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Expression And Purification ◽  
Active Peptide ◽  
Efficient Strategy
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