Premium
Biocatalysis of tyrosinase in chloroform medium, using selected phenolic substrates
Author(s) -
Kermasha Selim,
Tse Mara
Publication year - 2000
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/1097-4660(200006)75:6<475::aid-jctb237>3.0.co;2-2
Subject(s) - tyrosinase , chloroform , biocatalysis , chemistry , catechol , hydroquinone , bioconversion , substrate (aquarium) , organic chemistry , isoeugenol , chlorogenic acid , nuclear chemistry , enzyme , chromatography , catalysis , reaction mechanism , oceanography , eugenol , fermentation , geology
The biocatalysis of mushroom tyrosinase was optimized in chloroform medium using as substrates selected phenolic compounds, including chlorogenic acid (CA), p ‐aminophenol ( p AP) and hydroquinone (HQ). The specific activity of tyrosinase was found to be much higher in the chloroform medium than that obtained in the aqueous one. The optimal pH and temperature as well as other kinetic parameters for tyrosinase biocatalysis was also determined. The presence of catechol in the chloroform medium resulted in an increase in tyrosinase activity when CA was used as substrate; however, no activatory effect was found with p AP or HQ. The presence of ethylenediamine tetraacetic acid in the chloroform medium showed different effects on tyrosinase activity depending on the nature of the substrate. FT‐IR analyses confirmed the bioconversion of selected phenolic substrates into o ‐quinones by tyrosinase activity in the chloroform medium. © 2000 Society of Chemical Industry