Enhancing operational stability and exhibition of enzyme activity by removing water in the immobilized lipase‐catalyzed production of erythorbyl laurate |
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Authors: | Da Eun Lee Kyung Min Park Seung Jun Choi Jae‐Hoon Shim Pahn‐Shick Chang |
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Institution: | 1. Dept. of Agricultural Biotechnology, Seoul National University, , Seoul, 151–742 Republic of Korea;2. Dept. of Food Science and Technology, Seoul National University of Science and Technology, , Seoul, 139–743 Republic of Korea;3. Dept. of Food Science and Nutrition, Hallym University, , Chuncheon, 200–702 Republic of Korea;4. Center for Food Safety and Toxicology, Center for Food and Bioconvergence, and Research Institute for Agriculture and Life Sciences, Seoul National University, , Seoul, 151–742 Republic of Korea |
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Abstract: | Erythorbyl laurate was continuously synthesized by esterification in a packed‐bed enzyme reactor with immobilized lipase from Candida antarctica. Response surface methodology based on a five‐level three‐factor central composite design was adopted to optimize conditions for the enzymatic esterification. The reaction variables, such as reaction temperature (10–70°C), substrate molar ratio (lauric acid]/erythorbic acid], 5–15), and residence time (8–40 min) were evaluated and their optimum conditions were found to be 56.2°C, 14.3, and 24.2 min, respectively. Under the optimum conditions, the molar conversion yield was 83.4%, which was not significantly different (P < 0.05) from the value predicted (84.4%). Especially, continuous water removal by adsorption on an ion‐exchange resin in a packed‐bed enzyme reactor improved operational stability, resulting in prolongation of half‐life (2.02 times longer compared to the control without water‐removal system). Furthermore, in the case of batch‐type reactor, it exhibited significant increase in initial velocity of molar conversion from 1.58% to 2.04%/min. © 2013 American Institute of Chemical Engineers Biotechnol. Prog., 29:882–889, 2013 |
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Keywords: | erythorbyl laurate water removal immobilized lipase‐catalyzed esterification response surface methodology operational stability |
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