Enzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, Malaysia.
Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, Malaysia.
Biotechnol Appl Biochem. 2022 Dec;69(6):2599-2616. doi: 10.1002/bab.2309. Epub 2022 Feb 3.
Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from various bacterial species of the Bacillus genus such as Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and various other organisms. It is composed of 268-275 amino acid residues and is initially secreted in the precursor form, preprosubtilisin, which is composed of 29-residues signal peptide, 77-residues propeptide, and 275-residues active subtilisin. Subtilisin is known for the presence of high and low affinity calcium binding sites in its structure. Native subtilisin has general properties of thermostability, tolerance to neutral to high pH, broad specificity, and calcium-dependent stability, which contribute to the versatility of subtilisin applicability. Through protein engineering and immobilization technologies, many variants of subtilisin have been generated, which increase the applicability of subtilisin in various industries including detergent, food processing and packaging, synthesis of inhibitory peptides, therapeutic, and waste management applications.
由于其热稳定性和高 pH 值兼容性，枯草杆菌蛋白酶最著名的用途是作为洗涤剂的添加剂，根据 MEROPS 数据库，它被归类为丝氨酸蛋白酶。枯草杆菌蛋白酶通常从芽孢杆菌属的各种细菌物种中分离出来，如枯草芽孢杆菌、解淀粉芽孢杆菌、地衣芽孢杆菌和其他各种生物体。它由 268-275 个氨基酸残基组成，最初以前体形式分泌，即前原枯草杆菌蛋白酶，由 29 个残基的信号肽、77 个残基的前肽和 275 个残基的活性枯草杆菌蛋白酶组成。枯草杆菌蛋白酶的结构中存在高亲和性和低亲和性钙结合位点。天然枯草杆菌蛋白酶具有热稳定性、耐受中性到高 pH 值、广谱特异性和钙依赖性稳定性等一般特性，这有助于提高枯草杆菌蛋白酶的多功能适用性。通过蛋白质工程和固定化技术，已经产生了许多枯草杆菌蛋白酶的变体，这增加了枯草杆菌蛋白酶在包括洗涤剂、食品加工和包装、抑制肽合成、治疗和废物管理应用等各个行业的适用性。
