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Extraction penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with cetyl-trimethylammoniumbromide

Paper ID Volume ID Publish Year Pages File Format Full-Text
4942 260 2006 5 PDF Available
Title
Extraction penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with cetyl-trimethylammoniumbromide
Abstract

Cells were permeabilized with cetyl-trimethylammoniumbromide (CTAB) to extract penicillin G acylase (sp. Alcaligenes faecalis) in recombinant Escherichia coli. The optimum conditions were 0.5% (w/v) CTAB, 0.5 M ionic strength, pH 8.0 and at 4 °C for 28 h. The maximum relative enzyme activity obtained was 93.4%, and the specific activity increased about 1.6 times than that by ultrasonic fragmentation. Furthermore, CTAB-extracted enzyme solution had fine stability, and almost no activity decreased as the enzyme was preserved at 4 °C for 30 days. From these results, the method can be used as a high-performance system about the extraction of penicillin G acylase from A. faecalis that resides mainly in the outer periplasmic space of E. coli.

Keywords
Alcaligenes faecalis; Cell disruption; CTAB; Enzyme activity; Enzyme extraction; Penicillin G acylase
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Extraction penicillin G acylase from Alcaligenes faecalis in recombinant Escherichia coli with cetyl-trimethylammoniumbromide
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 32, Issue 1, 1 November 2006, Pages 56–60
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Full-text PDF Download
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Any Questions? feel free to contact us