Enzymatic synthesis of myristoyl disaccharides and their surface activity
Abstract The condensation of trehalose, maltose, cellobiose, sucrose, turanose, palatinose, lactose and melibiose with myristic acid by a lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) from Candida antarctica was examined at 60 °C in a mixture of pyridine and 2‐methyl‐2‐propanol (20/80 by vol.)....
| Published in: | Journal of the Science of Food and Agriculture |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2007
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/jsfa.2909 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjsfa.2909 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.2909 |
| Summary: | Abstract The condensation of trehalose, maltose, cellobiose, sucrose, turanose, palatinose, lactose and melibiose with myristic acid by a lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) from Candida antarctica was examined at 60 °C in a mixture of pyridine and 2‐methyl‐2‐propanol (20/80 by vol.). The reactivity of trehalose was the highest among the tested disaccharides, and maltose and palatinose followed. Cellobiose and lactose were poor substrates for condensation. Condensation of all the disaccharides except for cellobiose and lactose with myristic acid was carried out at various initial disaccharide concentrations to estimate the initial reaction rate. Plots of the initial rates for monomyristoyl disaccharide formation versus the initial disaccharide concentration normalized by the solubility of the disaccharide in the mixture indicated that palatinose was the best substrate, and that trehalose, turanose and maltose were the next best ones. The surface activity of the monoacyl disaccharides scarcely depended on the type of disaccharide. Copyright © 2007 Society of Chemical Industry |
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