Researcher Zheng Zhiming from the Institute of Technical Biology, Chinese Academy of Sciences Hefei Institute of Material Science and his research team have carried out in-depth and meticulous research on how to increase the activity of enzyme proteins in non-aqueous biocatalysis, combining non-aqueous enzyme catalysis with bioblotting , Realized the super-activation of tannase in non-aqueous phase system, improved the catalytic performance of tannase, and completed a series of studies on tannase non-aqueous phase catalyzed propyl gallate. This research work is supported by the Knowledge Innovation Project of the Chinese Academy of Sciences and the National High-Tech Research and Development Program. At present, 6 related research papers have been published.
Non-aqueous biocatalysis refers to the catalysis of enzymes in non-aqueous media. Compared with enzyme catalysis in aqueous solutions, enzyme catalysis in non-aqueous media can significantly improve the solubility of non-polar substrates or products and complete in aqueous solutions. Unsuccessful synthesis reactions, reduced product feedback inhibition of enzymes, and increased enantioselectivity of asymmetric reactions of chiral compounds. For example, a variety of organic compounds such as esters, peptides, and chiral alcohols can be obtained by enzyme-catalyzed reactions in organic media. Therefore, carrying out research on non-aqueous enzyme catalysis has important theoretical significance and application prospects.
Under the guidance of teacher Zheng, doctoral student Nie Guangjun took Aspergillus niger (Aspergillus niger) widely used in industry as the source of tannase enzyme, and the obtained tannase as the research object. The principle of relatively rigid conformation, using biological imprinting technology, has achieved the super-activation of tannase in non-aqueous systems.
The research group comprehensively applied enzyme Western blotting technology, antifreeze protection technology and immobilization technology to significantly improve the catalytic ester conversion performance in the organic phase of tanninase. The results show that pH adjustment, substrate imprinting and interface activation can significantly increase the tannin activity. Its ester conversion catalytic performance was improved by 123 times compared with the control, and the apparent activity of immobilized imprinted enzyme was nearly doubled. The combination of Triton X-100, mannose and Mg2 + reduced the loss of enzyme activity due to freeze-drying.
Through tannin enzyme imprinting technology and optimization of the reaction system, after batch catalysis and product coupling reaction, the substrate conversion rate reached 75%, which is higher than the related reports at home and abroad. In semi-continuous catalysis, the highest theoretical substrate conversion rate reaches 90%, which lays the foundation for achieving green, efficient preparation and industrial application of propyl gallate.
In addition, in order to explore the mechanism of imprinted enzymes to improve the efficiency of catalytic reactions, the research team carried out thermal and kinetic studies of enzymatic reactions. Within 40-60 ℃, the one-step ester conversion ΔG and ΔHd are lower than the free energy of the two-step reaction of tanninase hydrolysis and esterification, indicating that the one-step ester conversion efficiency is better than the two-step reaction. At 40 ℃, the Km of the imprinted enzyme was 0.054 mM, which was lower than the value reported in the literature, and the half-life was extended to 1710 h, which was significantly higher than that reported. This shows that the imprinting technique improves the affinity and stability of the tanninase substrate and improves the catalytic performance.
The reviewer of the article believes that it is feasible to study the bioactivation of super-activated tanninase, and analyze the key influencing factors and mechanism of tanninase imprinting process, which provides a reference for the establishment of bioimprinting methods in organic phase.
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