Enhancing operational stability and exhibition of enzyme activity by removing water in the immobilized lipase‐catalyzed production of erythorbyl laurate

• Published in: Biotechnology Progress
• Main Authors: Lee, Da Eun, Park, Kyung Min, Choi, Seung Jun, Shim, Jae‐Hoon, Chang, Pahn‐Shick
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2013
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1002/btpr.1745; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbtpr.1745; http://onlinelibrary.wiley.com/wol1/doi/10.1002/btpr.1745/fullpdf

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