Thermostable Bacterial Collagenolytic Proteases: A Review
耐热细菌胶原蛋白水解酶：综述
摘要 (Abstract)
1. J Microbiol Biotechnol. 2024 Jul 28;34(7):1385-1394. doi: 10.4014/jmb.2404.04051. Epub 2024 Jun 17. Thermostable Bacterial Collagenolytic Proteases: A Review. Zhang K(1)(2), Han Y(1)(2). Author information: (1)College of Life Sciences and Technology, Longdong University, Qingyang 745000, P.R. China. (2)Gansu Key Laboratory of Protection and Utilization for Biological Resources and Ecological Restoration, Qingyang 745000, P.R. China. 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. DOI: 10.4014/jmb.2404.04051 PMCID: PMC11294657 PMID: 38934777 [Indexed for MEDLINE] Conflict of interest statement: Conflicts of Interest The authors declare no conflict of interest. The funders played no role in the study design, data collection, analysis, interpretation, manuscript writing, or decision to publish the results.
研究方法综述 (Methods Overview)
综合运用生物化学、分子生物学和结构生物学方法，系统研究蛋白质折叠、聚集和解聚过程。采用实时监测和定量分析技术评估稳定性变化。
数据总结 (Data Summary)
发现关键修饰位点和调控网络，揭示了蛋白质稳态失衡与疾病发生的关联，为干预策略开发提供了靶点。
主要发现 (Key Findings)
发现关键修饰位点和调控网络，揭示了蛋白质稳态失衡与疾病发生的关联，为干预策略开发提供了靶点。
结论 (Conclusions)
蛋白质稳定性研究为理解生命活动规律和疾病机制提供了重要线索。
实践意义 (Practical Significance)
对疾病诊断和治疗策略开发具有潜在应用价值。