School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Jingkou District, Zhenjiang, 212013, Jiangsu, People's Republic of China.
Natural Sciences Unit, School of General Studies, University of Nigeria, Nsukka, 410002, Enugu State, Nigeria.
Appl Microbiol Biotechnol. 2023 Oct;107(19):5923-5934. doi: 10.1007/s00253-023-12721-y. Epub 2023 Aug 11.
Halophilic extracellular proteases offer promising application in various fields. Information on these prominent proteins including the synthesizing organisms, biochemical properties, domain organisation, purification, and application challenges has never been covered in recent reviews. Although extracellular proteases from bacteria pioneered the study of proteases in halophiles, progress is being made in proteases from halophilic archaea. Recent advances in extracellular proteases from archaea revealed that archaeal proteases are more robust and applicable. Extracellular proteases are composed of domains that determine their mechanisms of action. The intriguing domain structure of halophilic extracellular proteases consists of N-terminal domain, catalytic domain, and C-terminal extension. The role of C-terminal domains varies among different organisms. A high diversity of C-terminal domains would endow the proteases with diverse functions. With the development of genomics, culture-independent methods involving heterologous expression, affinity chromatography, and in vitro refolding are deployed with few challenges on purification and presenting novel research opportunities. Halophilic extracellular proteases have demonstrated remarkable potentials in industries such as detergent, leather, peptide synthesis, and biodegradation, with desirable properties and ability to withstand harsh industrial processes. KEY POINTS: • Halophilic extracellular proteases have robust properties suitable for applications. • A high diversity of C-terminal domains may endow proteases with diverse properties. • Novel protease extraction methods present novel application opportunities.
嗜盐细胞外蛋白酶在各个领域都有很好的应用前景。关于这些突出的蛋白质的信息，包括合成生物、生化特性、结构域组织、纯化和应用挑战，在最近的综述中从未涵盖过。尽管来自细菌的细胞外蛋白酶开创了嗜盐微生物蛋白酶的研究，但来自嗜盐古菌的蛋白酶的研究也取得了进展。最近在古菌细胞外蛋白酶方面的进展表明，古菌蛋白酶更具韧性和适用性。细胞外蛋白酶由决定其作用机制的结构域组成。嗜盐细胞外蛋白酶引人入胜的结构域结构由 N 端结构域、催化结构域和 C 端延伸组成。C 端结构域的作用在不同的生物体中有所不同。C 端结构域的高度多样性将赋予蛋白酶多样化的功能。随着基因组学的发展，涉及异源表达、亲和层析和体外重折叠的非培养方法得到了应用，在纯化方面的挑战较少，并提供了新的研究机会。嗜盐细胞外蛋白酶在洗涤剂、皮革、肽合成和生物降解等行业中表现出了显著的潜力，具有理想的性质和能够承受恶劣的工业过程的能力。要点：
嗜盐细胞外蛋白酶具有适合应用的稳健特性。
C 端结构域的高度多样性可能赋予蛋白酶多样化的特性。
新型蛋白酶提取方法提供了新的应用机会。
