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Reviews

Overview of strategies for developing high thermostability industrial enzymes: Discovery, mechanism, modification and challenges

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Abstract

Biocatalysts such as enzymes are environmentally friendly and have substrate specificity, which are preferred in the production of various industrial products. However, the strict reaction conditions in industry including high temperature, organic solvents, strong acids and bases and other harsh environments often destabilize enzymes, and thus substantially compromise their catalytic functions, and greatly restrict their applications in food, pharmaceutical, textile, bio-refining and feed industries. Therefore, developing industrial enzymes with high thermostability becomes very important in industry as thermozymes have more advantages under high temperature. Discovering new thermostable enzymes using genome sequencing, metagenomics and sample isolation from extreme environments, or performing molecular modification of the existing enzymes with poor thermostability using emerging protein engineering technology have become an effective means of obtaining thermozymes. Based on the thermozymes as biocatalytic chips in industry, this review systematically analyzes the ways to discover thermostable enzymes from extreme environment, clarifies various interaction forces that will affect thermal stability of enzymes, and proposes different strategies to improve enzymes’ thermostability. Furthermore, latest development in the thermal stability modification of industrial enzymes through rational design strategies is comprehensively introduced from structure-activity relationship point of view. Challenges and future research perspectives are put forward as well.

Disclosure statement

The authors declare that they do not have any actual or potential conflict of interest including any financial, personal or other relationships with other people or organizations within five years of beginning the submitted work that could inappropriately influence, or be perceived to influence, their work.

Additional information

Funding

This work was funded by National Natural Science Foundation of China (No. 31801583 and 31922073), the Natural Science Foundation of Jiangsu Province (No. BK20180607), the Key Technology R&D Program of Jiangsu Province (BE2019629), Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project (TSBICIP-KJGG-003), and the Key-Area Research and Development Program of Guangdong Province (2020B020226007).

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