Exploring the Antioxidant and Structural Properties of Black Bean Protein Hydrolysate and Its Peptide Fractions.
Exploring the Antioxidant and Structural Properties of Black Bean Protein Hydrolysate and Its Peptide Fractions.
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探索黑豆蛋白水解物及其肽组分的抗氧化和结构特性
DOI：
10.3389/fnut.2022.884537
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发表时间：
2022
影响因子：
5
通讯作者：
Liu, Yuanfa
中科院分区：
文献类型：
--
作者：
Chen, Yin;Zheng, Zhaojun;Ai, Zixuan;Zhang, Yan;Tan, Chin Ping;Liu, Yuanfa
关键词：
蛋白质酶解产物的表征一直是人们关注的焦点，但分子量分布对蛋白质酶解产物的影响尚不清楚。本研究旨在探讨蛋白质水解物及其多肽组分的理化特性和抗氧化特性。菠萝蛋白酶已被广泛用于黑豆蛋白的水解，通过响应面法（RSM）。最佳水解条件为：52°C，pH 7，E/S = 2.2（酶与底物的比例），水解时间4 h。在此条件下，褐藻胶水解物具有清除DPPH自由基和螯合Fe 2+的活性，IC 50值分别为100.08 ± 2.42和71.49 ± 0.81 μg/mL。这可能归因于结构特征，随不同的分子量分布而变化。有趣的是，在BPH及其肽组分中，注意到小于3 kDa的肽表现出最强的DPPH和ABTS自由基清除活性。更有趣的是，该肽级分（<3 kDa）可以显著延长向日葵油的诱导期，其分别增加至1.31倍。这可能是由于高比例的疏水性氨基酸。出乎意料的是，在3-10 kDa处测量的肽级分中观察到最佳的Fe 2+螯合活性，显示出与组氨酸和精氨酸的高度正相关。因此，这些鉴定的肽级分来源于黑豆蛋白，可用于食品强化作为天然抗氧化剂的替代品。
A great deal of attention has been paid to charactering the protein hydrolysates prepared by enzymatic hydrolysis, while the influence of molecular weight (MW) distributions on the resultant hydrolysates remains unclear. This study aimed to explore the physicochemical and antioxidant characteristics of protein hydrolysate and its peptide fractions. Bromelain has been commonly used to hydrolyze black bean protein via response surface methodology (RSM). The optimal hydrolysis parameters were observed at 52°C, pH 7, E/S ratio of 2.2 (ratio of enzyme to substrate), and 4 h. Under these parameters, the hydrolysate (BPH) presented DPPH radical scavenging activity and Fe2+ chelating activity with IC50 values of 100.08 ± 2.42 and 71.49 ± 0.81 μg/mL, respectively. This might be attributed to structural characteristics, varying with different molecular weight distributions. Interestingly, among BPH and its peptide fractions, peptides smaller than 3 kDa were noted to exhibit the strongest DPPH and ABTS radical scavenging activity. More intriguingly, this peptide fraction (<3 kDa) could predominantly prolong the induction period of sunflower oil, which was, respectively increased to 1.31 folds. This may be due to high proportions of hydrophobic amino acids. Unexpectedly, the optimal Fe2+ chelating activity was observed in the peptide fraction measuring at 3–10 kDa, showing highly positive correlations with histidine and arginine. These identified peptide fractions derived from black bean protein can therefore be employed for food fortification acting as natural antioxidant alternatives.
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