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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/17892
Title: Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase
Authors: N. Sriubolmas
W. Panbangred
S. Sriurairatana
V. Meevootisom
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Chemical Engineering;Immunology and Microbiology
Issue Date: 4-Jun-1997
Citation: Applied Microbiology and Biotechnology. Vol.47, No.4 (1997), 373-378
Abstract: Various concentrations of isopropyl β-D-thiogalactopyranoside (IPTG) were used to induce production of the enzyme penicillin G acylase by recombinant Escherichia coli harboring plasmid pQEA11. The plasmid pQEA11 carries a wild-type pga gene, which is under the control of the tac promoter and lacI(q). At low IPTG concentrations (0.025-0.1 mM), enzyme activity increased with increasing IPTG concentrations. At higher IPTG concentrations (0.2 and 0.5 mM), enzyme activity declined progressively. Examination of induced recombinant E. coli cells by transmission electron microscopy showed the presence of only periplasmic inclusion bodies at low IPTG concentrations (up to 0.1 mM) and both periplasmic and cytoplasmic inclusion bodies at high IPTG concentrations (0.2 mM and 0.5 mM). Results from sodium dodecyl sulfate/polyacrylamide gel electrophoresis and immunoblots of whole-cell proteins, membrane proteins and inclusion body proteins in these cells indicated that cytoplasmic inclusion bodies constituted an accumulation of pre-proenzyme (i.e., precursor polypeptide containing a signal peptide) and that periplasmic inclusion bodies constituted an accumulation of proenzyme (i.e., precursor polypeptide lacking a signal peptide).
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0030916974&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/17892
ISSN: 01757598
Appears in Collections:Scopus 1991-2000

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