Antihypertensive peptides from hydrolyzed proteins of Pleurotus spp.: Production, in vitro digestion and identification

IF 3.7 3区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Process Biochemistry Pub Date : 2024-11-23 DOI:10.1016/j.procbio.2024.11.027

Daniela Fernanda Lima de Carvalho Cavenaghi , Wander Miguel de Barros , Ruann Janser Soares de Castro

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引用次数: 0

Abstract

This study aimed to investigate in vitro antihypertensive property of protein hydrolysates from Pleurotus spp. mushrooms obtained through enzymatic hydrolysis. Flavourzyme™ 500 L, Alcalase™ 2.4 L and Neutrase™ 0.8 L were used alone and in combination using an experimental design of mixtures. Antihypertensive activity was determined by angiotensin-converting enzyme (ACE) inhibition and the simulated in vitro digestion was performed according to the INFOGEST protocol. Results showed that most of the protein hydrolysates obtained displayed higher ACE inhibitory activity than non-hydrolyzed protein, ranging from 15.76 % and 50.87 % inhibition. The highest ACE inhibition and the lowest TCA soluble protein content (52.09 %) were detected for the protein hydrolysates obtained by using the binary mixture of Flavourzyme™ 500 L and Alcalase™ 2.4 L in equal proportions. Hydrolysis kinetics showed no significant difference in ACE inhibitory activity between 20 and 120 minutes of enzymatic reaction. The fraction with molecular weight between 3 and 5 kDa obtained after ultrafiltration showed the most contribution for ACE inhibitory activity (47 % inhibition). After simulated digestion, the hydrolysates maintained a significant ACE inhibition capacity, indicating the resistance of the peptides to the action of gastrointestinal enzymes. Through proteomic analysis, 26 peptides were identified and the sequences LPILP, IPLLP, PLLPQ and VIQYDPPQ were considered potentially antihypertensive.

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侧耳菇水解蛋白抗高血压肽的制备、体外消化和鉴定

本研究旨在研究酶解平菇蛋白水解产物的体外降压特性。Flavourzyme™500 L、Alcalase™2.4 L和Neutrase™0.8 L单独或联合使用，采用混合实验设计。通过抑制血管紧张素转换酶（ACE）测定抗高血压活性，并根据INFOGEST方案进行模拟体外消化。结果表明，大多数蛋白水解产物的ACE抑制活性高于非水解蛋白，抑制率为15.76 %和50.87 %。Flavourzyme™500 L和Alcalase™2.4 L以等比例混合得到的蛋白水解产物，ACE抑制率最高，TCA可溶性蛋白含量最低（52.09 %）。水解动力学表明，酶促反应20和120 min时ACE抑制活性无显著差异。超滤后得到的分子量在3 ~ 5 kDa之间的部分对ACE抑制活性贡献最大（47 %）。模拟消化后，水解产物保持了显著的ACE抑制能力，表明肽对胃肠道酶的作用具有抗性。通过蛋白质组学分析，鉴定出26个多肽序列，认为LPILP、IPLLP、PLLPQ和VIQYDPPQ具有潜在的抗高血压作用。

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来源期刊

Process Biochemistry 生物-工程：化工

CiteScore

8.30

自引率

4.50%

发文量

374

审稿时长

53 days

期刊介绍： Process Biochemistry is an application-orientated research journal devoted to reporting advances with originality and novelty, in the science and technology of the processes involving bioactive molecules and living organisms. These processes concern the production of useful metabolites or materials, or the removal of toxic compounds using tools and methods of current biology and engineering. Its main areas of interest include novel bioprocesses and enabling technologies (such as nanobiotechnology, tissue engineering, directed evolution, metabolic engineering, systems biology, and synthetic biology) applicable in food (nutraceutical), healthcare (medical, pharmaceutical, cosmetic), energy (biofuels), environmental, and biorefinery industries and their underlying biological and engineering principles.