KMID : 1007520120210041209
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Food Science and Biotechnology 2012 Volume.21 No. 4 p.1209 ~ p.1215
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Optimal Production and Structural Characterization of Erythorbyl Laurate Obtained through Lipase-catalyzed Esterification
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Lee Da-Eun
Park Kyung-Min Choi Seung-Jun Chang Pahn-Shick
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Abstract
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Erythorbic acid, a stereoisomer of L-ascorbic acid, has been extensively used as an antioxidant but cannot be applied to lipid-based foods due to its poor lipophilicity. For this reason, synthesis of erythorbyl laurate (6-O-lauroyl-erythorbate) was achieved in acetonitrile using an immobilized lipase from Candida antarctica as a biocatalyst to increase its lipophilicity. Response surface methodology was used to optimize the erythorbyl laurate synthesis conditions in terms of enzyme content (1,000- 5,000 propyl laurate unit, PLU), molar ratio of lauric acid to erythorbic acid (5-25), and reaction temperature (25- 65¢ªC). The central composite experimental results showed the conditions for maximum molar conversion yield were as follows: enzyme content, 2,994 PLU; lauric acid to erythorbic acid molar ratio, 24.23; and reaction temperature, 53.03¢ªC. The maximum molar conversion yield reached 77.81%, which was in agreement with the predicted value (76.92%). The erythorbyl laurate was purified and identified by Fourier transform-infrared spectroscopy (FT-IR). This research could help to develop an economical method of synthesizing erythorbyl laurate for use as a novel foodgrade emulsifier with antioxidative activity.
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KEYWORD
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erythorbyl laurate, esterification, immobilized lipase, response surface methodology, antioxidant
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