Effect of hydrolysis time and peptide content on dpph* radical scavenging activity of bromelain- and papain-generated hydrolysates from defatted cocoa beans (Theobroma cacao l.) powder

O. A. Olanrewaju, S. Auwal
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Abstract

Enzyme generated protein hydrolysates have received considerable attention due to their numerous health effects. Among these, the anti-oxidative hydrolysates with DPPH* radical scavenging activity can play a significant role in the prevention of oxidative stress and the resulting chronic disease conditions such as cancer. In the present study, defatted cocoa beans (DCB) powder was dialyzed and then hydrolyzed for 8 h to produce DCB protein hydrolysates using two different proteases (bromelain and papain) at an optimum pH (6.8), temperature (400C) and enzyme/substrate ratio (1:50). The resulting DCB protein hydrolysates were evaluated for peptide content (PC) and DPPH* radical scavenging activity. The highest DPPH* radical scavenging activity of 78.07% and 53.04% were obtained at a peptide content of 4.85 mg/dL and 3.13 mg/dL for the bromelain- and papain-generated DCB protein hydrolysates at 6 h hydrolysis time, respectively. The effect of hydrolysis time and peptide content on the DPPH* radical scavenging activity of the DCB protein hydrolysates was then studied. The result obtained indicated positive correlation between the DPPH* radical scavenging activity of both bromelain- and papain-generated DCB protein hydrolysates to their peptide content based on Pearson’s correlation analysis with R2 values of 0.946 and 0.772, respectively.
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水解时间和多肽含量对脱脂可可豆粉菠萝蛋白酶和木瓜蛋白酶水解产物清除dpph*自由基活性的影响
酶生成的蛋白质水解物由于其众多的健康影响而受到了相当大的关注。其中,具有DPPH*自由基清除活性的抗氧化水解物在预防氧化应激和由此产生的慢性疾病如癌症中发挥重要作用。本研究采用两种不同的蛋白酶(菠萝蛋白酶和木瓜蛋白酶),在最佳pH(6.8)、温度(400℃)和酶/底物比(1:50)的条件下,对脱脂可可豆(DCB)粉末进行透析,水解8 h,得到DCB蛋白水解产物。对得到的DCB蛋白水解产物进行肽含量(PC)和DPPH*自由基清除活性的评估。当肽含量为4.85 mg/dL和3.13 mg/dL时,菠萝蛋白酶和木瓜蛋白酶生成的DCB蛋白水解时间为6 h,其DPPH*自由基清除率分别为78.07%和53.04%。研究水解时间和多肽含量对DCB蛋白水解产物清除DPPH*自由基活性的影响。结果表明,菠萝蛋白酶和木瓜蛋白酶生成的DCB蛋白水解产物的DPPH*自由基清除活性与其肽含量呈正相关,Pearson相关分析R2分别为0.946和0.772。
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