Background: Microbial γ-glutamyl transpeptidases (GGTs) have been exploited in biotechnological, pharmaceutical, and food sectors for the synthesis of various γ-glutamyl compounds. But, till date, no bacterial GGTs are commercially available in the market because of lower levels of production from various sources. In the current study, production of GGT from Bacillus licheniformis ER15 was investigated to achieve high GGT titers.
Results: Hyperproduction of GGT from B. licheniformis ER15 was achieved with 6.4-fold enhancement (7921.2 ± 198.7 U/L) by optimization of culture medium following one-variable-at-a-time strategy and statistical approaches. Medium consisting of NaHPO: 0.32% (w/v); KHPO: 0.15% (w/v); starch: 0.1% (w/v); soybean meal: 0.5% (w/v); NaCl: 4.0% (w/v), and MgCl: 5 mM was found to be optimal for maximum GGT titers. Maximum GGT titers were obtained, in the optimized medium at 37°C and 200 rpm, after 40 h. It was noteworthy that GGT production was a linear function of sodium chloride concentration, as observed during response surface methodology. While investigating the role of NaCl on GGT production, it was found that NaCl drastically decreased subtilisin concentration and indirectly increasing GGT recovery.
Conclusion: B. licheniformis ER15 is proved to be a potential candidate for large-scale production of GGT enzyme and its commercialization.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1080/10826068.2016.1188314 | DOI Listing |
Enzyme Microb Technol
September 2018
Department of Microbiology, University of Delhi South Campus, New Delhi 110021, India. Electronic address:
Increasing demand of microbial γ-glutamyl transpeptidase (GGT) in food and pharmaceutical sectors raised the need for process development for high level production of the enzyme. In this respect, GGT from Bacillus licheniformis ER15 (SBLGGT) was cloned along with its native secretion signal and expressed in E. coli using different expression vectors.
View Article and Find Full Text PDFJ Biotechnol
May 2017
Department of Microbiology, University of Delhi South Campus, New Delhi 110021, India. Electronic address:
γ-Glutamyl transpeptidase (GGT) catalyzes the transfer of the γ-glutamyl moiety from donor compounds such as l-glutamine (Gln) and glutathione (GSH) to an acceptor. During the biosynthesis of various γ-glutamyl-containing compounds using GGT enzyme, auto-transpeptidation reaction leads to the formation of unwanted byproducts. Therefore, in order to alter the auto-transpeptidase activity of the GGT enzyme, the binding affinity of Gln should be modified.
View Article and Find Full Text PDFPrep Biochem Biotechnol
February 2017
a Department of Microbiology , University of Delhi, South Campus , New Delhi , India.
Background: Microbial γ-glutamyl transpeptidases (GGTs) have been exploited in biotechnological, pharmaceutical, and food sectors for the synthesis of various γ-glutamyl compounds. But, till date, no bacterial GGTs are commercially available in the market because of lower levels of production from various sources. In the current study, production of GGT from Bacillus licheniformis ER15 was investigated to achieve high GGT titers.
View Article and Find Full Text PDFInt J Biol Macromol
October 2016
Department of Microbiology, University of Delhi, South Campus, New Delhi 110021, India. Electronic address:
Gamma-glutamyl transpeptidase enzyme, from Bacillus licheniformis ER15 (BLGGT), was produced extracellularly using a complex medium with high enzyme titers. Enzyme was concentrated and purified using ultra-filtration and ion exchange chromatography, respectively, with a purification fold of 4.6 and 50.
View Article and Find Full Text PDFJ Agric Food Chem
September 2014
Department of Microbiology, University of Delhi, South Campus, New Delhi 110021, India.
Recombinant γ-glutamyl transpeptidase (rBLGGT) from Bacillus licheniformis ER-15 was purified to homogeneity by ion-exchange chromatography. Molecular masses of large and small subunits were 42 and 22 kDa, respectively. The enzyme was optimally active at pH 9.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!