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In vivo immobilization of d-hydantoinase in Escherichia coli

Paper ID Volume ID Publish Year Pages File Format Full-Text
20538 43179 2014 4 PDF Available
Title
In vivo immobilization of d-hydantoinase in Escherichia coli
Abstract

d-p-Hydroxyphenylglycine (d-HPG) is a precursor required for the synthesis of semi-synthetic antibiotics. This unnatural amino acid can be produced by a transformation reaction mediated by d-hydantoinase (d-HDT) and d-amidohydrolase. In this study, a method was developed to integrate production and immobilization of recombinant d-HDT in vivo. This was approached by first fusion of the gene encoding d-HDT with phaP (encoding phasin) of Ralstonia eutropha H16. The fusion gene was then expressed in the Escherichia coli strain that carried a heterologous synthetic pathway for polyhydroxyalkanoate (PHA). As a result, d-HDT was found to associate with isolated PHA granules. Further characterization illustrated that d-HDT immobilized on PHA exhibited the maximum activity at pH 9 and 60°C and had a half-life of 95 h at 40°C. Moreover, PHA-bound d-HDT could be reused for 8 times with the conversion yield exceeding 90%. Overall, it illustrates the feasibility of this approach to facilitate in vivo immobilization of enzymes in heterologous E. coli strain, which may open a new avenue of enzyme application in industry.

Keywords
In vivo immobilization; d-Hydantoinase; Polyhydroxyalkanoate; Phasin; d-p-Hydroxyphenylglycine
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In vivo immobilization of d-hydantoinase in Escherichia coli
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 118, Issue 1, July 2014, Pages 78–81
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