Refolding with Simultaneous Purification of Recombinant Serratia marcescens Lipase by One-Step Ultrasonication Process

Yin, Yue-Cai; Li, Hongquan; Wu, Xin-Sen

doi:10.1007/s12010-019-03172-1

Cited by 7 publications

(6 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result is interesting due to the fact that recombinant proteins are usually expressed intracellularly in E. coli (Fakruddin et al, 2013;Ma et al, 2020). Moreover, in various studies, recombinant S. marcesces lipase in E. coli were reported to be expressed intracellularly (Su et al, 2014;Mohammadi et al, 2016;Chen et al, 2017;Yin et al, 2020) As previously reported, S. marcescens LII61 lipase exhibited high activity (Ni'matuzahroh et al, 2017;Renjana et al, 2017). However, the industrial application of the lipase is hampered by the pathogenicity of S. marcescens.…”

Section: Discussionmentioning

confidence: 55%

Expression of Recombinant Lipase from Serratia marcescens LII61 in Escherichia coli

2022

JJBS

View full text Add to dashboard Cite

Recombinant lipase encoding gene of Serratia marcescens LII61 has been successfully expressed in Escherichia coli. The gene was amplified from genomic DNA of S. marcescens LII61 by PCR method using lipase specific primers. The amplified DNA was then subsequently inserted in pGEM ® -T easy vector and transformed into E. coli JM109. The inserted DNA fragment in the plasmid was analyzed for studying the lipase gene sequence. The recombinant gene was subcloned in pET-28b(+) vector/ E. coli BL21(DE3) system. The positive clones were selected by growing E. coli cells in antibiotic medium and lipase-specific medium. The analysis of recombinant DNA showed that the lipase gene of S. marcescens LII61 was 1845 bp in size. The inserted gene in the pGEM-T easy vector was composed of 1842 bp lipase gene and flanked by several restriction enzyme as stated on the map vector. The recombinant E. coli BL21 (DE3) showed a fluorescent orange color on LB-IPTG-rhodamine B-olive oil agar plate, indicated that the recombinant bacteria were able to express the lipase gene from S. marcescens LII61. This report is the first endeavor on cloning and expression of lipase from Indonesian isolate of S. marcescens.

show abstract

Section: Discussionmentioning

confidence: 55%

Expression of Recombinant Lipase from Serratia marcescens LII61 in Escherichia coli

2022

JJBS

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 55%

“…Accumulating pieces of evidence have shown that COVID-19 infection could be spread from person-toperson. This was corroborated by cases that took place within families and among people who did not visit the wet animal market in Wuhan (Wu et al, 2020). Transmission from individual to individual occurs mainly through direct contact or via droplets released by coughing or sneezing from infected person (Rothan and Byrareddy, 2020).…”

Section: Transmission Of Sars-cov-2 In Sub-sahara Africamentioning

confidence: 89%

Untitled

2022

JJBS

View full text Add to dashboard Cite

Study areas include cell biology, genomics, microbiology, immunology, molecular biology, biochemistry, embryology, immunogenetics, cell a n d tissue culture, molecular ecology, genetic engineering and biological engineering, bioremediation and biodegradation, bioinformatics, biotechnology regulations, gene therapy, organismal biology, microbial and environmental biotechnology, marine sciences. The JJBS welcomes the submission of manuscripts that meet the general criteria of significance and academic excellence. All articles published in JJBS are peerreviewed. Papers will be published approximately in one to two months after acceptance.

show abstract

“…Lipase from S. marcescens ECU1010 catalyzed production of (−)-MPGM by the enzymatic resolution of trans-3-(4′-methoxyphenyl)glycidic acid methyl ester ((±)-MPGM) with chitosan in an isopropyl ether water biphasic system (Zhao et al, 2010). Overexpression of S. marcescens lipase in E. coli often promotes inclusion bodies, which is one of the major problems in industrial recombinant protein production [174,175]. A simple and efficient method for refolding with simultaneous purification of S. marcescens lipase in E. coli in the production of (−)-MPGM has been described with an overall yield of 41.5% and ee of 99% [175].…”

Section: Pharmaceutical Applications Of Recombinant Lipasesmentioning

confidence: 99%

“…Overexpression of S. marcescens lipase in E. coli often promotes inclusion bodies, which is one of the major problems in industrial recombinant protein production [174,175]. A simple and efficient method for refolding with simultaneous purification of S. marcescens lipase in E. coli in the production of (−)-MPGM has been described with an overall yield of 41.5% and ee of 99% [175]. Figure 7 shows a lipase-catalyzed scheme of the synthetic process of diltiazem.…”

Section: Pharmaceutical Applications Of Recombinant Lipasesmentioning

confidence: 99%

Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

et al. 2020

View full text Add to dashboard Cite

Lipases are one of the most used enzymes in the pharmaceutical industry due to their efficiency in organic syntheses, mainly in the production of enantiopure drugs. From an industrial viewpoint, the selection of an efficient expression system and host for recombinant lipase production is highly important. The most used hosts are Escherichia coli and Komagataella phaffii (previously known as Pichia pastoris) and less often reported Bacillus and Aspergillus strains. The use of efficient expression systems to overproduce homologous or heterologous lipases often require the use of strong promoters and the co-expression of chaperones. Protein engineering techniques, including rational design and directed evolution, are the most reported strategies for improving lipase characteristics. Additionally, lipases can be immobilized in different supports that enable improved properties and enzyme reuse. Here, we review approaches for strain and protein engineering, immobilization and the application of lipases in the pharmaceutical industry.

show abstract

Refolding with Simultaneous Purification of Recombinant Serratia marcescens Lipase by One-Step Ultrasonication Process

Cited by 7 publications

References 44 publications

Expression of Recombinant Lipase from Serratia marcescens LII61 in Escherichia coli

Expression of Recombinant Lipase from Serratia marcescens LII61 in Escherichia coli

Untitled

Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

Contact Info

Product

Resources

About