耐热细菌胶原溶解蛋白酶:综述。

IF 2.5 4区 生物学 Q3 BIOTECHNOLOGY & APPLIED MICROBIOLOGY
Journal of microbiology and biotechnology Pub Date : 2024-07-28 Epub Date: 2024-06-17 DOI:10.4014/jmb.2404.04051
Kui Zhang, Yapeng Han
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引用次数: 0

摘要

胶原蛋白分解蛋白酶广泛应用于食品、医疗、制药、化妆品和纺织行业。嗜中性胶原蛋白酶在生理条件下具有胶原蛋白分解活性,但由于其热稳定性差,在高温下有效降解富含胶原蛋白的废物(如鱼鳞中的胶原蛋白)时受到限制。细菌胶原溶解蛋白酶属于不同的蛋白酶家族,包括细菌胶原溶解金属蛋白酶 M9 和细菌胶原溶解丝氨酸蛋白酶家族 S1、S8 和 S53。值得注意的是,胶原蛋白溶解蛋白酶的 C 端结构域,如前肽酶 C 端结构域、多囊肾病样结构域、胶原蛋白结合结构域、丙蛋白转化酶结构域和β-果冻卷结构域,都具有胶原蛋白结合或膨胀活性。这些活性可诱导胶原蛋白或酶活性位点发生构象变化,从而提高胶原蛋白的降解效率。热稳定性细菌胶原蛋白溶解蛋白酶在高温下发挥作用,其优点是可以提高降解效率,因为热变性的胶原蛋白更容易被蛋白水解,而且可以将微生物污染的风险降至最低。迄今为止,只有少数几种嗜热菌衍生的胶原蛋白溶解蛋白酶得到了表征。TSS是一种可恒温且耐盐碱的类枯草蛋白丝氨酸胶原蛋白溶解蛋白酶,在60°C时具有很高的胶原蛋白溶解活性。在这篇综述中,我们介绍并总结了目前对来自不同微生物的恒温和嗜中性胶原蛋白溶解蛋白酶的分类和命名及其 C 端结构域的功能作用的研究。此外,我们还分析了每个家族中恒温胶原蛋白溶解蛋白酶的裂解特异性,并全面讨论了恒温胶原蛋白溶解蛋白酶 TSS。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Thermostable Bacterial Collagenolytic Proteases: A Review.

Collagenolytic proteases are widely used in the food, medical, pharmaceutical, cosmetic, and textile industries. Mesophilic collagenases exhibit collagenolytic activity under physiological conditions, but have limitations in efficiently degrading collagen-rich wastes, such as collagen from fish scales, at high temperatures due to their poor thermostability. Bacterial collagenolytic proteases are members of various proteinase families, including the bacterial collagenolytic metalloproteinase M9 and the bacterial collagenolytic serine proteinase families S1, S8, and S53. Notably, the C-terminal domains of collagenolytic proteases, such as the pre-peptidase C-terminal domain, the polycystic kidney disease-like domain, the collagen-binding domain, the proprotein convertase domain, and the β-jelly roll domain, exhibit collagen-binding or -swelling activity. These activities can induce conformational changes in collagen or the enzyme active sites, thereby enhancing the collagen-degrading efficiency. In addition, thermostable bacterial collagenolytic proteases can function at high temperatures, which increases their degradation efficiency since heat-denatured collagen is more susceptible to proteolysis and minimizes the risk of microbial contamination. To date, only a few thermophile-derived collagenolytic proteases have been characterized. TSS, a thermostable and halotolerant subtilisin-like serine collagenolytic protease, exhibits high collagenolytic activity at 60°C. In this review, we present and summarize the current research on A) the classification and nomenclature of thermostable and mesophilic collagenolytic proteases derived from diverse microorganisms, and B) the functional roles of their C-terminal domains. Furthermore, we analyze the cleavage specificity of the thermostable collagenolytic proteases within each family and comprehensively discuss the thermostable collagenolytic protease TSS.

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来源期刊
Journal of microbiology and biotechnology
Journal of microbiology and biotechnology BIOTECHNOLOGY & APPLIED MICROBIOLOGY-MICROBIOLOGY
CiteScore
5.50
自引率
3.60%
发文量
151
审稿时长
2 months
期刊介绍: The Journal of Microbiology and Biotechnology (JMB) is a monthly international journal devoted to the advancement and dissemination of scientific knowledge pertaining to microbiology, biotechnology, and related academic disciplines. It covers various scientific and technological aspects of Molecular and Cellular Microbiology, Environmental Microbiology and Biotechnology, Food Biotechnology, and Biotechnology and Bioengineering (subcategories are listed below). Launched in March 1991, the JMB is published by the Korean Society for Microbiology and Biotechnology (KMB) and distributed worldwide.
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