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Chaperone-mediated folding and maturation of the Penicillin acylase precursor in the cytoplasm of Escherichia coli

Article Abstract:

A study on expression of the leaderless pac gene (LL pac) that lacks the coding region for the signal peptide of penicillin acylase (PAC) in Escherichia coli was conducted. The results suggested that folding/misfolding of proPAC can be a major step limiting the overproduction of PAC in Escherichia coli and that the problem can be resolved through the search for appropriate chaperones for coexpression.

Author: Yali Xu, Scharer, Jeno M., Chiao-Ling Weng, Murray Moo-Young, Chou, C. Perry, Narayanan, Niju, Ming-Yi Hsieh, Anderson, William A.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Genetic aspects, Bacterial genetics, Signal peptides

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Fermentative utilization of glycerol by Escherichia coli and its implications for the production of fuels and chemicals

Article Abstract:

The utilization of the carbon source in the absence of electron acceptors is described. The implications of the results for the production of reduced chemicals and fuels are described by coproducing ethanol plus formic acid and ethanol plus hydrogen from glycerol at yields approaching their theoretical maximum.

Author: Gonzalez, Ramon, Murarka, Abhishek, Dharmadi, Yandi, Yazdani, Syed Shams
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2008
Manufacturing processes, All Other Basic Organic Chemical Manufacturing, CHEMICALS AND ALLIED PRODUCTS, Industrial organic chemicals, not elsewhere classified, Ethanol, Ethyl Alcohol Manufacturing, Glycerine, Physiological aspects, Production processes, Fermentation, Alcohol, Glycerol, Chemical properties, Alcohol, Denatured, Glycerin

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Stabilization of Penicillin G acylase from Escherichia coli: site directed mutagenesis of the protein surface to increase multipoint covalent attachment

Article Abstract:

An improved strategy for enzyme stability that consists of using site-directed mutagenesis to increase multipoint covalent attachment is studied. Three mutations on Penicillin acylase surface from Escherichia coli were performed and results were analyzed, discussed and tabulated.

Author: Abian, Olga; Fernandez-Lafuente, Roberto, Grazu, Valeria; Guisan, Jose Manuel, Hermoso, Juan, Gonzalez, Ramon, Garcia, Jose Luis
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
Causes of, Chemical bonds, Penicillin G

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Subjects list: Research, Escherichia coli
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