文献类型：期刊文献

中文题名：响应面法优化牡蛎可溶性多肽提取及其ACE抑制活性研究

英文题名：Optimization of Oyster Soluble Peptide Extraction Using Response Surface Methodology and Preliminary Investigation of Its ACE Inhibitory Activity

作者：李团章[1];杨菲[1];钟怡琳[1];李晓磊[1];卢昊天[1];赖智杰[1];卢健豪[1];李乐凡[1];谌素华[1]

机构：[1]广东海洋大学化学与环境学院,广东湛江524088

年份：2025

期号：21

起止页码：13

中文期刊名：农产品加工

外文期刊名：Farm Products Processing

基金：大学生创新创业训练计划项目(CXXL2023198)。

语种：中文

中文关键词：香港牡蛎;牡蛎可溶性多肽;响应面法;酶解工艺;ACE抑制活性

外文关键词：crassostrea hongkongensis;oyster soluble peptide;response surface methodology;enzymatic hydrolysis process;ACE inhibitory activity

中文摘要：通过响应面法优化牡蛎可溶性多肽(Oyster soluble peptide,OSP)的提取工艺并对其ACE抑制活性进行初步探究。以香港牡蛎(Crassostrea hongkongensis)为原料,基于筛选出的最佳蛋白酶,进行单因素试验和方差分析,考查酶解反应温度、pH值、料液比、酶添加量和酶解时间5个因素;以ACE抑制率为响应指标,对料液比、酶解反应温度和酶解酶解时间3个关键因素进行优化。利用紫外和红外光谱对所提取的OSP的结构特征进行初步鉴定。筛选出最佳蛋白酶为动物蛋白酶,利用该酶对牡蛎原浆进行水解得到的可溶性ACE抑制多肽质量浓度为44.58 mg/m L,水解度为22.28%。通过响应面法得出ACE抑制肽最佳提取工艺为酶解时间3.98 h,酶解反应温度50.55℃,料液比19∶31(g∶m L),该条件下ACE抑制率高达51.2%。紫外和红外光谱分析表明,所制得的具备高ACE抑制活性的OSP结构完整。研究得到的最佳OSP提取工艺可制备高ACE活性的可溶性肽,在高提取率和高活性牡蛎多肽提取工艺的生产上具有重要意义。

外文摘要：Response surface methodology was employed to optimize the extraction process of oyster soluble peptides(OSP)and evaluate their angiotensin-converting enzyme(ACE)inhibitory activity.A one-way analysis of variance(ANOVA)was conducted to assess the impact of five variables.Reaction temperature,pH,feed-liquid ratio,enzyme concentration,and enzyme time,using the optimal protease selected from Hong Kong oyster(Crassostrea hongkongensis).Three key factors-feed-liquid ratio,enzyme reaction temperature,and enzyme time were identified and optimized,with ACE inhibition serving as the response indicator.The structural characteristics of the extracted OSPs were preliminarily identified through UV and IR spectroscopy.Animal protease was identified as the most effective enzyme,yielding an ACE inhibitory peptide concentration of 44.58 mg/mL with a hydrolysis degree of 22.28%.The optimal conditions for peptide extraction were determined using RSM,enzyme digestion time of 3.98 h,enzyme reaction temperature of 50.55℃,and a material-to-liquid ratio of 19∶31(g∶mL).Under these conditions,the ACE inhibition rate reached 51.2%.UV and IR spectral analyses confirmed that the OSP with high ACE inhibitory activity retained a structurally intact form under these conditions.The optimized OSP extraction process developed in this study provided a means of producing soluble peptides with high ACE inhibitory activity,which was significant for developing efficient oyster peptide extraction methods with both high extraction rates and bioactivity.