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以贻贝为原料,制备具有血管紧张素Ⅰ转换酶(ACE)抑制作用的活性肽。采用水解度DH、蛋白质回收率及ACE抑制活性为指标,筛选水解贻贝粗蛋白的最适酶种;通过响应面分析(RSM)对水解贻贝粗蛋白的工艺条件进行优化;探讨水解度(DH)与ACE抑制活性的关系;利用HPLC方法分析活性肽的相对分子质量分布。试验结果表明碱性蛋白酶Alcalase 2.4L是水解贻贝粗蛋白的最适酶种;碱性蛋白酶在[E]/[S]1.64、pH9.12、温度57℃水解条件下,酶解物的ACE抑制作用最强,其DH26.41%,IC5034.64g/mL。就贻贝粗蛋白的水解而言,控制水解度为25%～30%为宜。碱性蛋白酶水解贻贝粗蛋白所得活性肽,主要是以相对分子质量较小的短肽组成,其中,相对分子质量在1000Da以内的占90.42%。本研究结果表明以贻贝为原料,可以开发具有显著ACE抑制活性的降血压肽。
Using mussels as raw materials, an active peptide with inhibition of angiotensin I converting enzyme (ACE) was prepared. The optimum enzymes for hydrolyzing mussel crude protein were screened by DH, protein recovery rate and ACE inhibitory activity. The optimal hydrolysis conditions of mussel crude protein were determined by response surface methodology (RSM) DH) with ACE inhibitory activity; the relative molecular weight distribution of active peptides was analyzed by HPLC method. The results showed that alkaline protease Alcalase 2.4L was the most suitable enzyme for hydrolyzing mussel. The enzymatic hydrolysis of alkaline protease under the condition of [E] / [S] 1.64, pH9.12 and temperature 57 ℃, The strongest inhibitory effect was DH26.41% and IC5034.64g / mL. As far as the hydrolysis of mussel crude protein is concerned, it is advisable to control the degree of hydrolysis to 25% to 30%. Alkaline protease hydrolyzed crude protein from mussel was mainly composed of short peptides of relatively small molecular weight, of which the relative molecular mass was less than 1000Da, accounting for 90.42%. The results of this study suggest that using hypothalamus as a starting material, a hypotensive peptide with significant ACE inhibitory activity can be developed.