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绵羊奶酪乳清水解物作为具有抗氧化和血管紧张素转换酶抑制活性的生物活性肽来源。

Hydrolysates of sheep cheese whey as a source of bioactive peptides with antioxidant and angiotensin-converting enzyme inhibitory activities.

作者信息

Corrêa Ana Paula Folmer, Daroit Daniel Joner, Fontoura Roberta, Meira Stela Maris Meister, Segalin Jeferson, Brandelli Adriano

机构信息

Laboratório de Bioquímica e Microbiologia Aplicada, Instituto de Ciência e Tecnologia de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul (UFRGS), 91501-970 Porto Alegre, RS, Brazil.

Universidade Federal da Fronteira Sul (UFFS), Campus Cerro Largo, 97900-000 Cerro Largo, RS, Brazil.

出版信息

Peptides. 2014 Nov;61:48-55. doi: 10.1016/j.peptides.2014.09.001. Epub 2014 Sep 10.

DOI:10.1016/j.peptides.2014.09.001
PMID:25218972
Abstract

Enzymatic proteolysis may be employed to release bioactive peptides, which have been investigated for potential benefits from both technological and human health perspectives. In this study, sheep cheese whey (SCW) was hydrolyzed with a protease preparation from Bacillus sp. P7, and the hydrolysates were evaluated for antioxidant and angiotensin I-converting enzyme (ACE)-inhibitory activities. Soluble protein and free amino acids increased during hydrolysis of SCW for up to 4h. Antioxidant activity of hydrolysates, evaluated by the 2,2'azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid radical scavenging method, increased 3.2-fold from 0 h (15.9%) to 6h of hydrolysis (51.3%). Maximum Fe(2+) chelation was reached in 3h hydrolysates, and the reducing power peaked at 1h of hydrolysis, representing 6.2 and 2.1-fold increase, respectively, when compared to that of non-hydrolyzed SCW. ACE inhibition by SCW (12%) was improved through hydrolysis, reaching maximal values (55% inhibition) in 4h, although 42% inhibition was already observed after 1h hydrolysis. The peptide LAFNPTQLEGQCHV, derived from β-lactoglobulin, was identified from 4-h hydrolysates. Such a biotechnological approach might be an interesting strategy for SCW processing, potentially contributing to the management and valorization of this abundant dairy byproduct.

摘要

酶促蛋白水解可用于释放生物活性肽,从技术和人类健康角度对其潜在益处进行了研究。在本研究中,用芽孢杆菌属P7的蛋白酶制剂水解绵羊奶酪乳清(SCW),并评估水解产物的抗氧化和血管紧张素I转换酶(ACE)抑制活性。在SCW水解长达4小时的过程中,可溶性蛋白和游离氨基酸增加。通过2,2'-联氮-双-(3-乙基苯并噻唑啉-6-磺酸)自由基清除法评估,水解产物的抗氧化活性从水解0小时(15.9%)到6小时增加了3.2倍(51.3%)。3小时水解产物达到最大铁(II)螯合能力,还原能力在水解1小时达到峰值,与未水解的SCW相比,分别增加了6.2倍和2.1倍。SCW对ACE的抑制率为12%,通过水解得到改善,在4小时达到最大值(55%抑制),尽管在水解1小时后已观察到42%的抑制率。从4小时水解产物中鉴定出源自β-乳球蛋白的肽LAFNPTQLEGQCHV。这种生物技术方法可能是SCW加工的一种有趣策略,可能有助于对这种丰富的乳制品副产品进行管理和增值利用。

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