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源自微生物的冷适应酶的研究进展。

Advances in cold-adapted enzymes derived from microorganisms.

作者信息

Liu Yehui, Zhang Na, Ma Jie, Zhou Yuqi, Wei Qiang, Tian Chunjie, Fang Yi, Zhong Rongzhen, Chen Guang, Zhang Sitong

机构信息

College of Life Science, Jilin Agricultural University, Changchun, China.

Key Laboratory of Straw Comprehensive Utilization and Black Soil Conservation, Ministry of Education, Changchun, China.

出版信息

Front Microbiol. 2023 Apr 26;14:1152847. doi: 10.3389/fmicb.2023.1152847. eCollection 2023.

DOI:10.3389/fmicb.2023.1152847
PMID:37180232
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10169661/
Abstract

Cold-adapted enzymes, produced in cold-adapted organisms, are a class of enzyme with catalytic activity at low temperatures, high temperature sensitivity, and the ability to adapt to cold stimulation. These enzymes are largely derived from animals, plants, and microorganisms in polar areas, mountains, and the deep sea. With the rapid development of modern biotechnology, cold-adapted enzymes have been implemented in human and other animal food production, the protection and restoration of environments, and fundamental biological research, among other areas. Cold-adapted enzymes derived from microorganisms have attracted much attention because of their short production cycles, high yield, and simple separation and purification, compared with cold-adapted enzymes derived from plants and animals. In this review we discuss various types of cold-adapted enzyme from cold-adapted microorganisms, along with associated applications, catalytic mechanisms, and molecular modification methods, to establish foundation for the theoretical research and application of cold-adapted enzymes.

摘要

冷适应酶是在冷适应生物体中产生的一类酶,它们在低温下具有催化活性,对高温敏感,并且能够适应冷刺激。这些酶主要来源于极地、山区和深海中的动物、植物和微生物。随着现代生物技术的快速发展,冷适应酶已应用于人类和其他动物食品生产、环境保护与修复以及基础生物学研究等诸多领域。与来源于植物和动物的冷适应酶相比,来源于微生物的冷适应酶因其生产周期短、产量高以及分离纯化简单而备受关注。在本综述中,我们讨论了来自冷适应微生物的各种冷适应酶,以及相关的应用、催化机制和分子修饰方法,为冷适应酶的理论研究和应用奠定基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/e32a4cf6943b/fmicb-14-1152847-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/f49ec937b7ec/fmicb-14-1152847-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/41348af16f66/fmicb-14-1152847-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/ff60982c0ae1/fmicb-14-1152847-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/fb8f31d90a06/fmicb-14-1152847-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/addd02084bf5/fmicb-14-1152847-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/89c39176ef34/fmicb-14-1152847-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/2d57bcaefec1/fmicb-14-1152847-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/62e12cfeaeb0/fmicb-14-1152847-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/9db1a6c42b33/fmicb-14-1152847-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/e32a4cf6943b/fmicb-14-1152847-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/f49ec937b7ec/fmicb-14-1152847-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/41348af16f66/fmicb-14-1152847-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/ff60982c0ae1/fmicb-14-1152847-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/fb8f31d90a06/fmicb-14-1152847-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/addd02084bf5/fmicb-14-1152847-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/89c39176ef34/fmicb-14-1152847-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/2d57bcaefec1/fmicb-14-1152847-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/62e12cfeaeb0/fmicb-14-1152847-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/9db1a6c42b33/fmicb-14-1152847-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bc67/10169661/e32a4cf6943b/fmicb-14-1152847-g010.jpg

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