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Cold-adapted enzymes: mechanisms, engineering and biotechnological application

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Abstract

Most cold-adapted enzymes display high catalytic activity at low temperatures (20–25 °C) and can still maintain more than 40–50% of their maximum activity at lower temperatures (0–10 °C) but are inactivated after a moderate increase in temperature. The activity of some cold-adapted enzymes increases significantly in the presence of high salt concentrations and metal ions. Interestingly, we also observed that some cold-adapted enzymes have a wide range of optimum temperatures, exhibiting not only maximum activity under low-temperature conditions but also the ability to maintain high enzyme activity under high-temperature conditions, which is a novel feature of cold-adapted enzymes. This unique property of cold-adapted enzymes is generally attractive for biotechnological and industrial applications because these enzymes can reduce energy consumption and the chance of microbial contamination, thereby lowering the production costs and maintaining the flavor, taste and quality of foods. How high catalytic activity is maintained at low temperatures remains unknown. The relationship between the structure of cold-adapted enzymes and their activity, flexibility and stability is complex, and thus far, a unified explanation has not been provided. Herein, we systematically review the sources, catalytic characteristics and cold adaptation of enzymes from four enzymes categories systematically and discuss how these properties may be exploited in biotechnology. A thorough understanding of the properties, catalytic mechanisms, and engineering of cold-adapted enzymes is critical for future biotechnological applications in the detergent industry and food and beverage industries.

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Data availability

The datasets used or analyzed during the current study are available from the corresponding author on reasonable request.

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Funding

Financial support from the National Natural Science Foundation of China (Grant no. 31570054), the State Key Laboratory of Microbial Technology Open Projects Fund (Project nos. M2021-09, M2022-06), the Open Project Program for Key Laboratory of Fermentation Engineering (Ministry of Education) (202105FE08), and the Postgraduate Research Innovation Project 2023 for Hubei University of Technology are gratefully acknowledged.

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  1. Cooperative Innovation Center of Industrial Fermentation (Ministry of Education and Hubei Province), Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei Key Laboratory of Industrial Microbiology, National “111” Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan, 430068, China

    Yan Liu, Kaizhi Jia, Hongyang Chen, Zhulin Wang & Liwen Zhu

  2. State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, China

    Wei Zhao

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  1. Yan Liu
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JKZ and ZW designed the study and coordinated the work. LY and CHY prepared all figures and tables. LY and ZLW wrote and revised the manuscript. JKZ and ZLW supervised. WZL and LY collated supplementary data for the manuscript. All authors have read and agreed to the published version of the manuscript.

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Correspondence to Liwen Zhu.

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Table S1: Phylogenetic comparison of four types of cold-adapted enzymes from different sources based on amino acid sequences, Fig. S1: Phylogenetic comparison of four types of cold-adapted enzymes from different sources based on amino acid sequences. (DOCX 914 KB)

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Liu, Y., Jia, K., Chen, H. et al. Cold-adapted enzymes: mechanisms, engineering and biotechnological application. Bioprocess Biosyst Eng 46, 1399–1410 (2023). https://doi.org/10.1007/s00449-023-02904-2

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