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Expression of a cholesterol oxidase gene from Arthrobacter simplex in Escherichia coli and Pichia pastoris

Paper ID Volume ID Publish Year Pages File Format Full-Text
18532 42725 2006 7 PDF Available
Title
Expression of a cholesterol oxidase gene from Arthrobacter simplex in Escherichia coli and Pichia pastoris
Abstract

The gene (choAA), encoding cholesterol oxidase from Arthrobacter simplex F2, was cloned and sequenced by polymerase chain reaction. The gene consists of 1653 base pairs and encodes a protein of 551 amino acids (aa). N-terminal sequence analysis of the extracellular cholesterol oxidase of A. simplex F2 confirmed that the mature enzyme consists of 502 aa with a predicted molecular mass of 54,269 Da, and is translated with a 49 aa signal sequence. The structure gene for ChoAA was cloned and expressed efficiently in Escherichia coli and Pichia pastoris. The deletion of the choAA signal sequence was favorable for the expression of extracellular cholesterol oxidase by P. pastoris.

Keywords
Cholesterol oxidase; Arthrobacter simplex; Escherichia coli; Pichia pastoris
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Expression of a cholesterol oxidase gene from Arthrobacter simplex in Escherichia coli and Pichia pastoris
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 4, 2 August 2006, Pages 854–860
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
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