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Incremental truncation of PHA synthases results in altered product specificity

Paper ID Volume ID Publish Year Pages File Format Full-Text
17139 42646 2012 5 PDF Available
Title
Incremental truncation of PHA synthases results in altered product specificity
Abstract

PHA synthase is the key enzyme involved in the biosynthesis of microbial polymers, polyhydroxyalkanoates (PHA). In this study, we created a hybrid library of PHA synthase gene with different crossover points by an incremental truncation method between the C-terminal fragments of the phaCCn (phaC from Cupriavidus necator) and the N-terminal fragments of the phaC1Pa (phaC from Pseudomonas aeruginosa). As the truncation of the hybrid enzyme increased, the in vivo PHB synthesis ability of the hybrids declined gradually. PHA synthase PhaCCn with a deletion on N-terminal up to 83 amino acid residues showed no synthase activity. While with the removal of up to 270 amino acids from the N-terminus, the activity of the truncated PhaCCn could be complemented by the N-terminus of PhaC1Pa. Three of the hybrid enzymes W188, W235 and W272 (named by the deleted nucleic acid number) were found to have altered product specificities.

► A hybrid library of PHA synthases (PhbCCn and PhaC1Pa) was constructed by incremental truncation method. ► The activity of the truncated PhaCCn could be complemented by the N-terminus of PhaC1Pa. ► Three of the hybrid enzymes were found to have altered product specificity.

Keywords
Polyhydroxyalkanoates; PHA synthase; Hybrid; Copolymer; Incremental truncation; Library
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 50, Issues 6–7, 10 May 2012, Pages 293–297
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