Solvent effects in horseradish peroxidase-catalyzed polyphenol synthesis

Autor:	John E. Walker, Joseph A. Akkara, Suprabhat Chatterjee, David L. Kaplan, Madhu S. R. Ayyagari
Rok vydání:	2002
Předmět:	Circular dichroism biology Chemistry Dispersity Bioengineering Photochemistry Applied Microbiology and Biotechnology Biochemistry Horseradish peroxidase Enzyme structure Solvent Polymerization biology.protein Organic chemistry Solubility Solvent effects Biotechnology
Zdroj:	Enzyme and Microbial Technology. 30:3-9
ISSN:	0141-0229
DOI:	10.1016/s0141-0229(01)00438-0
Popis:	Enzyme-solvent-monomer molecular interactions and their effect on horseradish peroxidase-catalyzed polymerization of m-cresol in ethanol/water mixtures were studied. A mechanistic approach of the effect of reaction medium composition on the poly (m-cresol) molecular weight and polydispersity was elucidated from the standpoint molecular interactions. Solvent effects on the enzyme activity and structure were studied by reaction kinetics and spectroscopic methods including UV-vis, fluorescence, circular dichroism and electron paramagnetic spectroscopy (EPR). In view of the results from these studies, the observed polymer molecular weight profile could be deduced from the solubility of the polymer as well as the partitioning of the monomer between solvent and the enzyme active site.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::376ff98ae33e1c4581aaecf6a1b252eb https://doi.org/10.1016/s0141-0229(01)00438-0 Zobrazit plný text záznamu Full Text from ScienceDirect