Stabilization of interface-binding chloroperoxidase

Ravindrabharathi Narayanan, Ping Wang

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Chloroperoxidase was conjugated with polystyrene to form an interface-binding biocatalyst. The polymer-enzyme conjugate enabled a unique interfacial biocatalysis for styrene epoxidation reaction. The stability of the interface-assembled Chloroperoxidase against the inactivation effect of hydrogen peroxide under emulsified conditions was examined. It was observed that in situ generation of hydrogen peroxide using glucose oxidase increased the operational stability of the enzyme, while polyethyleneimine increased the storage stability chloroperoxidase in hydrogen peroxide solution. The addition of polyethylene glycol, however, interestingly increased both operational and storage stability of chloroperoxidase with higher productivity as compared to reactions without enzyme stabilization.

Original languageEnglish (US)
Title of host publication05AIChE
Subtitle of host publication2005 AIChE Annual Meeting and Fall Showcase, Conference Proceedings
Number of pages1
StatePublished - Dec 1 2005
Event05AIChE: 2005 AIChE Annual Meeting and Fall Showcase - Cincinnati, OH, United States
Duration: Oct 30 2005Nov 4 2005

Other

Other05AIChE: 2005 AIChE Annual Meeting and Fall Showcase
CountryUnited States
CityCincinnati, OH
Period10/30/0511/4/05

Fingerprint Dive into the research topics of 'Stabilization of interface-binding chloroperoxidase'. Together they form a unique fingerprint.

Cite this