Journal
CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION
Volume 63, Issue 14, Pages 2057-2073Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/10408398.2021.1970508
Keywords
Thermostability; protein engineering; industrial enzymes; extreme environment; interaction force
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This article introduces the importance of discovering new thermostable enzymes using methods such as genome sequencing, metagenomics, and sample isolation from extreme environments, as well as the use of protein engineering technology to modify existing enzymes. It also proposes strategies to improve the thermostability of enzymes.
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.
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