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Strategies for producing recombinant sucrose phosphorylase originating from Bifidobacterium longum in Escherichia coli JM109

Paper ID Volume ID Publish Year Pages File Format Full-Text
35528 45094 2008 7 PDF Available
Title
Strategies for producing recombinant sucrose phosphorylase originating from Bifidobacterium longum in Escherichia coli JM109
Abstract

The optimal production conditions of sucrose phosphorylase (SPase), which catalyzes transferring sugars to polyphenols, cloned from the anaerobic Bifidobacterium longum into Escherichia coli JM109 were studied. Without isopropyl-β-d-thiogalactopyranoside (IPTG), the segregational stability of the recombinant plasmids was maintained over 80%, even in the absence of antibiotic pressure. When IPTG was added, the plasmids were completely lost after 80 generations. The structural stability of the plasmid was found to be well-maintained. The earlier induction with 10 μM of IPTG at 37 °C was best for the high volumetric activity of the enzyme. The maximal activity of SPase per cell mass was found to be much higher in M9 media than in LB media. In batch bioreactor culture, the maximum values for cell mass concentration, volumetric activity of SPase, and specific activity of SPase based on total soluble protein were 0.84 g l−1, 2.65 U ml−1, and 18.14 U mg−1 of soluble protein, respectively.

Keywords
Sucrose phosphorylase; Bifidobacterium longum; Escherichia coli; Plasmid stability; Heterologous expression; Inclusion body
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Strategies for producing recombinant sucrose phosphorylase originating from Bifidobacterium longum in Escherichia coli JM109
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 8, August 2008, Pages 822–828
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
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us