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Optimization of catechol production by membrane‐immobilized polyphenol oxidase: A modeling approach
Author(s) -
Boshoff A.,
Burton M. H.,
Burton S. G.
Publication year - 2003
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.10695
Subject(s) - catechol , polyphenol oxidase , chemistry , biotransformation , phenols , catechol oxidase , polyphenol , membrane , tyrosinase , phenol , substrate (aquarium) , immobilized enzyme , enzyme , organic chemistry , biochemistry , chromatography , antioxidant , biology , peroxidase , ecology
Although previous research has focused on phenol removal efficiencies using polyphenol oxidase in nonimmobilized and immobilized forms, there has been little consideration of the use of polyphenol oxidase in a biotransformation system for the production of catechols. In this study, polyphenol oxidase was successfully immobilized on various synthetic membranes and used to convert phenolic substrates to catechol products. A neural network model was developed and used to model the rates of substrate utilization and catechol production for both nonimmobilized and immobilized polyphenol oxidase. The results indicate that the biotransformation of the phenols to their corresponding catechols was strongly influenced by the immobilization support, resulting in differing yields of catechols. Hydrophilic membranes were found to be the most suitable immobilization supports for catechol production. The successful biocatalytic production of 3‐methylcatechol, 4‐methylcatechol, catechol, and 4‐chlorocatechol is demonstrated. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 83: 1–7, 2003.