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High-level production penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with optimization of carbon sources

Paper ID Volume ID Publish Year Pages File Format Full-Text
18730 42738 2007 5 PDF Available
Title
High-level production penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with optimization of carbon sources
Abstract

Different carbon sources were investigated for overproduction penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli strains. The results indicated that the enzyme was optimally produced with 45 g/l of dextrin, and about 43,385 and 79,880 U/l for the highest enzyme activities were obtained in batch cultivations of shaken flasks and a 3.7 l bioreactor, respectively. Active site titration and SDS-PAGE electrophoretic analysis demonstrated that the maximum yield of the active enzyme was 2.54 g/l, which was about 40% of total soluble proteins. The highest specific activity of A. faecalis penicillin G acylase obtained was above 10 U/mg protein, and there was almost no plasmid lost in the whole batch cultivations. Furthermore, the cultivation process was relatively simple and suitable for large-scale production.

Keywords
Alcaligenes faecalis; Batch cultivation; Carbon source; Overexpression; Penicillin G acylase
First Page Preview
High-level production penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with optimization of carbon sources
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 41, Issue 3, 2 August 2007, Pages 326–330
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering