Cloning, Expression, and Purification of the His6-Tagged Thermostable β-Galactosidase from Pyrococcus woesei in Escherichia coli and Some Properties of the Isolated Enzyme

2000 ◽  
Vol 19 (1) ◽  
pp. 107-112 ◽  
Author(s):  
Sławomir Dąabrowski ◽  
Gabriela Sobiewska ◽  
Jadwiga Maciuńska ◽  
Józef Synowiecki ◽  
Józef Kur
Keyword(s):  
Escherichia Coli ◽  
Expression And Purification ◽  
Pyrococcus Woesei

Expression and Purification of Bioactive High-Purity Recombinant Mouse SPP1 in Escherichia coli

2014 ◽  
Vol 173 (2) ◽  
pp. 421-432 ◽  
Author(s):  
Yunsheng Yuan ◽  
Xiyuan Zhang ◽  
Shunyan Weng ◽  
Wen Guan ◽  
Di Xiang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Purity ◽  
Expression And Purification ◽  
Recombinant Mouse

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.

scholarly journals Expression and purification of recombinant lyase gp17 from the LSB-1 phage in Escherichia coli

2015 ◽  
Vol 30 (1) ◽  
pp. 69-72 ◽  
Author(s):  
Taiwu Wang ◽  
Hui Lin ◽  
Lu Zhang ◽  
Guorong Huang ◽  
Long Wu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Expression And Purification

Escherichia coli expression and purification of recombinant dog albumin, a cross-reactive animal allergen

2000 ◽  
Vol 105 (2) ◽  
pp. 279-285 ◽  
Author(s):  
Budhi Pandjaitan ◽  
Ines Swoboda ◽  
Franziska Brandejsky-Pichler ◽  
Helmut Rumpold ◽  
Rudolf Valenta ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Expression And Purification ◽  
Escherichia Coli Expression ◽  
Animal Allergen
Sign in / Sign up

Export Citation Format

Share Document