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Abstract：
The Angiotensin-I-converting enzyme (ACE) is a peptidase with a significant role in the regulation of blood pressure. Within this work, a systematic review on the enzymatic preparation of Angiotensin-I-Converting Enzyme inhibitory (ACEi) peptides is presented. The systematic review is conducted by following PRISMA guidelines. Soybeans and velvet beans are known to have high protein contents that make them suitable as sources of parent proteins for the production of ACEi peptides. Endopeptidase is commonly used in the preparation of soybean-based ACEi peptides, whereas for velvet bean, a combination of both endo- and exopeptidase is frequently used. Soybean glycinin is the preferred substrate for the preparation of ACEi peptides. It contains proline as one of its major amino acids, which exhibits a potent significance in inhibiting ACE. The best enzymatic treatments for producing ACEi peptides from soybean are as follows: proteolytic activity by Protease P (Amano-P from Aspergillus sp.), a temperature of 37 °C, a reaction time of 18 h, pH 8.2, and an E/S ratio of 2%. On the other hand, the best enzymatic conditions for producing peptide hydrolysates with high ACEi activity are through sequential hydrolytic activity by the combination of pepsin-pancreatic, an E/S ratio for each enzyme is 10%, the temperature and reaction time for each proteolysis are 37 °C and 0.74 h, respectively, pH for pepsin is 2.0, whereas for pancreatin it is 7.0. As an underutilized pulse, the studies on the enzymatic hydrolysis of velvet bean proteins in producing ACEi peptides are limited. Conclusively, the activity of soybean-based ACEi peptides is found to depend on their molecular sizes, the amino acid residues, and positions. Hydrophobic amino acids with nonpolar side chains, positively charged, branched, and cyclic or aromatic residues are generally preferred for ACEi peptides.
摘要：
血管紧张素I转换酶（ACE）是一种在血压调节中起重要作用的肽酶。在这项工作中，提出了关于血管紧张素I转换酶抑制（ACEi）肽的酶法制备的系统综述。系统审查是按照PRISMA指南进行的。已知大豆和天鹅绒豆具有高蛋白质含量,这使得它们适合作为用于生产ACEi肽的亲本蛋白质的来源。内肽酶通常用于制备大豆基ACEi肽，而对于天鹅绒豆，内肽酶和外肽酶的组合经常使用。大豆大豆球蛋白是制备ACEi肽的优选底物。它含有脯氨酸作为其主要氨基酸之一，在抑制ACE方面表现出有效的意义。从大豆生产ACEi肽的最佳酶处理如下：蛋白酶P的蛋白水解活性（来自曲霉属的Amano-P。),温度为37°C，反应时间为18小时，pH为8.2,E/S比为2%。另一方面,生产具有高ACEi活性的肽水解产物的最佳酶促条件是通过胃蛋白酶-胰腺组合的顺序水解活性，每种酶的E/S比为10%，每次蛋白水解的温度和反应时间为37°C和0.74h，分别,胃蛋白酶的pH为2.0,而胰酶制剂的pH为7.0。作为一个未充分利用的脉冲，有关天鹅绒豆蛋白酶水解生产ACEi肽的研究有限。最后，发现大豆基ACEi肽的活性取决于它们的分子大小，氨基酸残基，和位置。具有非极性侧链的疏水性氨基酸，带正电荷,分支，和环状或芳族残基通常优选用于ACEi肽。
