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Enzyme glycation influences product yields during oligosaccharide synthesis by reverse hydrolysis

Maitin, V. and Rastall, R.A. (2004) Enzyme glycation influences product yields during oligosaccharide synthesis by reverse hydrolysis. Journal of Molecular Catalysis B-Enzymatic, 30 (5-6). pp. 195-202. ISSN 1381-1177

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To link to this item DOI: 10.1016/j.molcatb.2004.05.004

Abstract/Summary

Possible evidence is presented for Maillard glycation of enzymes during oligosaccharide synthesis by reverse hydrolysis. In 70% (w/v) mannose solutions, 1,2-alpha-mannosidase from Penicillium citrinum lost 40% and alpha-mannosidase from almonds lost 60% activity at 55 degreesC over 2 weeks. Oligosaccharide yields were 15 and 45% respectively. Higher molecular weight glycation adducts were formed in a time-dependent manner as seen by MALDI-TOF. Inhibitors of the Maillard. reaction were able to partially alleviate these effects resulting in reduced loss of enzyme activity and oligosaccharide yield increases of 27-53% relative to the control. (C) 2004 Elsevier B.V. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13174
Uncontrolled Keywords:Maillard reaction, alpha-mannosidase, enzymatic synthesis, oligosaccharide synthesis, reverse hydrolysis, ALPHA-MANNOSIDASE REACTION, PROTEIN CROSS-LINKING, MAILLARD REACTION, PENICILLIUM-CITRINUM, ASPERGILLUS-PHOENICIS, AMINO-ACIDS, INACTIVATION, INHIBITORS, KINETICS, 1,2-ALPHA-MANNOSIDASE

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