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Catalytic esterification performance of protease in micro-aqueous system

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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.

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Abbreviations

Ms :

Sucrose mass

Mp :

Products mass

Sp :

Products peak area

Ss :

Sucrose peak area

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Acknowledgements

The authors would like to thank professor Junqing Qian for all the feedstock.

Funding

This research project was financially supported by China's National Key Research and Development Program (Grant Number 2016YFD0400803).

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Correspondence to Junqing Qian.

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The authors declare that they have no conflict of interest regarding the publication of this paper.

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Qian, J., Gou, L., Zhao, X. et al. Catalytic esterification performance of protease in micro-aqueous system. Biotechnol Lett 42, 2157–2167 (2020). https://doi.org/10.1007/s10529-020-02965-3

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  • DOI: https://doi.org/10.1007/s10529-020-02965-3

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