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A highly pH-stable phytase from Yersinia kristeensenii: Cloning, expression, and characterization

Paper ID Volume ID Publish Year Pages File Format Full-Text
17844 42700 2008 7 PDF Available
Title
A highly pH-stable phytase from Yersinia kristeensenii: Cloning, expression, and characterization
Abstract

The gene appA, encoding a phytase from Yersinia kristeensenii, was cloned and heterologously expressed in Pichia pastoris. The open reading frame of appA comprised 1326 bp encoding a protein of 441 amino acids including a 24-amino acid signal peptide. The encoded phytase, APPA, was 87% identical to the phytase from Y. intermedia but was <52% identical to other histidine acid phosphatases. The purified recombinant phytase had an optimal activity at 55 °C and pH 4.5, and it exhibited enzymatic activity between pH 2.0 and 6.5, with a specific activity of 2656 U mg−1 at pH 4.5 and 37 °C. r-APPA retained more than 90% of its initial activity after being incubated under varying pH conditions (pH 1.5–11.0) at 37 °C for 3 h. r-APPA was resistant to heat inactivation, as it retained 46% of its initial activity after incubation at 80 °C for 10 min. r-APPA was effective for the hydrolysis of phytate phosphorus from soybean meal in vitro. Comparison of r-APPA with other well-known phytases suggests that the Y. kristeensenii phytase would be an attractive enzyme for feed industry use.

Keywords
Phytase; pH stable; Histidine acid phosphatase; Yersinia kristeensenii; Pichia pastoris
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A highly pH-stable phytase from Yersinia kristeensenii: Cloning, expression, and characterization
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 42, Issue 6, 5 May 2008, Pages 499–505
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