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Cross‐Linked Enzyme Aggregates of Chloroperoxidase: Synthesis, Optimization and Characterization
Author(s) -
Perez Daniel I.,
van Rantwijk Fred,
Sheldon Roger A.
Publication year - 2009
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200900303
Subject(s) - chemistry , coprecipitation , enzyme , hydrogen peroxide , enzyme assay , biochemistry , organic chemistry
In this study we have optimized the conditions to precipitate and cross‐link the enzyme chloroperoxidase (EC 1.11.1.10) from Caldariomyces fumago (CPO) using 1,2‐dimethoxyethane as the precipitating agent. The coprecipitation of the enzyme with albumin and pentaethylenehexamine was needed for optimum results, presumably due to the low number of lysines available in CPO. The enzyme was immobilized with an activity recovery of 68%. The cross‐linked enzyme aggregate showed higher temperature and pH stability, and better hydrogen peroxide tolerance than the free enzyme.