Optimization of catechol production by membrane-immobilized polyphenol oxidase: a modeling approach

• Published in: Biotechnology and bioengineering 2003-07, Vol.83 (1), p.1-7
• Main Authors: Boshoff, A, Burton, M.H, Burton, S.G
• Format: Article
• Language: English
• Subjects: Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; catechol oxidase; Catechol Oxidase - chemistry; catechol production; Catechols - chemical synthesis; Computer Simulation; Enzyme Activation; Enzymes, Immobilized - chemistry; Fundamental and applied biological sciences. Psychology; immobilization supports; immobilized enzymes; Membranes, Artificial; Methods. Procedures. Technologies; Models, Chemical; neural network modeling; neural networks; Neural Networks (Computer); Phenols - chemistry; polyphenol oxidase; Quality Control; Substrate Specificity
• ISSN: 0006-3592; 1097-0290
• DOI: 10.1002/bit.10695

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.