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 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.
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| Item Type | Article |
| URI | https://reading-clone.eprints-hosting.org/id/eprint/13174 |
| Identification Number/DOI | 10.1016/j.molcatb.2004.05.004 |
| Refereed | Yes |
| Divisions | Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences |
| 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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