Reverse hydrolysis reaction in aqueous medium without any cosolvent

Autor: Alain Guibert, Xavier Cameleyre, Alain Bouchu, Didier Combes
Rok vydání: 1997
Předmět:
Zdroj: Applied Biochemistry and Biotechnology. 62:61-69
ISSN: 1559-0291
0273-2289
Popis: The synthesis of L-tyrosine fructosyl ester, from fructose and L-tyrosine methyl ester, was carried out by a transesterification reaction catalyzed by α-chymotrypsin in water without cosolvent. The effect of fructose concentration and temperature for the transesterification reaction were determined on both specific activities and product yield. The influence of the presence of fructose has been studied regarding α-chymotrypsin and L-tyrosine fructosyl ester stabilities. It appeared that an increase of temperature enhanced enzyme activity but slumped the product yield because of the very weak stability of tyrosine fructosyl ester.
Databáze: OpenAIRE