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Maillard reactions and increased enzyme inactivation during oligosaccharide synthesis by a hyperthermophilic glycosidase
Author(s) -
Bruins M. E.,
Van Hellemond E. W.,
Janssen A. E. M.,
Boom R. M.
Publication year - 2002
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.10498
Subject(s) - maillard reaction , pyrococcus furiosus , chemistry , oligosaccharide , enzyme , lactose , biochemistry , browning , glycoside hydrolase , archaea , gene
The thermostable Pyrococcus furiosus β‐glycosidase was used for oligosaccharide production from lactose in a kinetically controlled reaction. Our experiments showed that higher temperatures are beneficial for the absolute as well as relative oligosaccharide yield. However, at reaction temperatures of 80°C and higher, the inactivation rate of the enzyme in the presence of sugars was increased by a factor of 2 compared to the inactivation rate in the absence of sugars. This increased enzyme inactivation was caused by the occurrence of Maillard reactions between the sugar and the enzyme. The browning of our reaction mixture due to Maillard reactions was modeled by a cascade of a zeroth‐ and first‐order reaction and related to enzyme inactivation. From these results we conclude that modification of only a small number of amino groups already gives complete inactivation of the enzyme. © 2003 Wiley Periodicals. Biotechnol Bioeng 81:546–552, 2003.