Catalytic esterification performance of protease in micro-aqueous system
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ORIGINAL RESEARCH PAPER
Catalytic esterification performance of protease in micro-aqueous system Junqing Qian . Lihong Gou . Xiaohua Zhao . Changyan Zhao . Hui Guo . Yudong Shan
Received: 4 February 2020 / Accepted: 8 July 2020 Ó Springer Nature B.V. 2020
Abstract Objective To evaluate the catalytic esterification performance of proteases in micro-aqueous systems and to study the suitable conditions for maintaining protease activity. Results It was found that the protease showed better enzyme catalytic activity in the micro-aqueous phase containing 4% boric acid-borax buffer than that of the pure organic phase. The protease activity was easily activated by 0.20 M boric acid-borax buffer, and the enzyme activity was still high for a long time in alkaline environment (pH 8.40–9.60) and under the temperature of 40–55 °C. Experiments using protease and Candida lipase to synthesize sucrose-6-ethyl ester showed that protease had better esterification activity than Candida lipase in the micro-aqueous phase. Keywords Catalytic esterification Micro-aqueous phase Protease
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s10529-020-02965-3) contains supplementary material, which is available to authorized users. J. Qian (&) L. Gou X. Zhao C. Zhao H. Guo Y. Shan College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310014, People’s Republic of China e-mail: [email protected]
Abbreviations Ms Sucrose mass Mp Products mass Sp Products peak area Ss Sucrose peak area
Introduction The traditional view was that the presence of water or even trace amounts of water in the esterification system caused hydrolysis of the esterification product and reduced the esterification yield. However, recent literature studies (Liu et al. 2011; Karboune et al. 2018) had shown that enzymatic esterification could be carried out in the mixture of organic solvents with water or buffering system and water content would affect the dissolution of the water-soluble substrate and the regioselectivity of the enzyme. Moreover, the microaqueous phase has a wider application range and more suitable substrate than the organic phase in esterification system. Li and Feng (2013) reported the lipase was utilized for the resolution of the model compound (R, S)-1-phenyl ethanol in heptane, the heptane/[Bmim]PF6 mixture, lipase exhibited catalysis activity at the heptane-ionic liquid interface when the mixture of heptane/[Bmim]PF6 was used as the reaction solvent. The effects of ionic liquids (ILs) as cosolvents on the enzymatic synthesis of 6-O-acetyl sucrose by Aspergillus oryzae fructosyltransferase
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Biotechnol Lett
(AoFT) was carried out (wei et al. 2016), and sucrose ester conversion rate and 6-O-acetyl sucrose yield increased 2.90-fold and 3.18-fold under the optimum reaction solvent of [Dmim][PF6]-phosphate buffer (20:80, v/v) system. To the best of our knowledge, the transesterification of proteases in the microaqueous pha
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