豆类种子蛋白水解物的功能、抗氧化、抗炎和抗糖尿病特性研究

IF 4.6 Q1 CHEMISTRY, APPLIED
Taiwo Scholes Adewole , Michael Chukwuemeka Bieni , Gbenga Emmanuel Ogundepo , Oludele Olayemi Odekanyin , Adenike Kuku
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引用次数: 0

摘要

植物衍生水解物因其随之而来的功能和生物活性特性,正在成为治疗各种疾病的有前途的药物。本研究调查了塞内加尔红豆杉(Erythrina senegalensis)和亚赤藜(Vigna subtenarrea)种子水解物的功能、抗氧化、抗炎和抗糖尿病特性。通过碱性溶解分离粗蛋白,然后酸沉淀至等电点。使用胰蛋白酶和胃蛋白酶以 1:8 的酶-底物比(v/v)水解各自的蛋白质分离物 1-9 小时。同时,消化 1 和 9 小时的塞内加尔胃蛋白酶和胰蛋白酶水解物分别显示出最高的 1,1-二苯基-2-苦基肼自由基清除能力(10-IC50 = 2.959 mg/mL)和总抗氧化能力(7.243 mgAAE/g)。相应地,水解 5 小时的塞内加尔胃蛋白酶和胰蛋白酶水解物通过抑制黄嘌呤氧化酶和脂氧合酶的活性,表现出最有效的抗炎活性,IC50 分别为 0.161 ± 0.111 和 0.018 ± 0.011 mg/mL。经 5 小时水解的 V. subterranea 的胰蛋白酶水解物能有效抑制α-淀粉酶和α-葡萄糖苷酶的活性,IC50 分别为 0.297 ± 0.060 和 0.314 ± 0.064 mg/mL。总体而言,与 V. subterranea 的水解物相比,E. senegalensis 的胃蛋白酶和胰蛋白酶水解物具有明显的功能性生物活性。本研究的结论是,这两种种子都可以作为潜在功能性生物活性肽的独特基质,具有治疗糖尿病的前景。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Investigation of functional, antioxidant, anti-inflammatory, and antidiabetic properties of legume seed protein hydrolysates

Plant-derived hydrolysates are emerging as promising agents in the management of diverse ailments due to their ensuing functional and bioactive properties. This study investigated the functional, antioxidant, anti-inflammatory, and antidiabetic properties of hydrolysates from Erythrina senegalensis and Vigna subtenarrea seeds. Crude proteins were isolated via alkaline solubilization, followed by acid precipitation to the isoelectric point. Respective protein isolates were hydrolyzed using trypsin and pepsin at an enzyme-substrate ratio of 1:8 (v/v) for 1–9 h. Pepsin hydrolysates after 9 h elicited the highest solubilities of 95.54 % and 94.24 % at pH 13, while, pepsin and trypsin hydrolysates of E. senegalensis digested for 1 and 9 h displayed the highest 1,1-diphenyl-2-picrylhydrazyl radical-scavenging (10-IC50 = 2.959 mg/mL) and total antioxidant capacity (7.243 mgAAE/g), respectively. Correspondingly, pepsin and trypsin hydrolysates of E. senegalensis hydrolyzed for 5 h demonstrated the most potent anti-inflammatory activities by cogently inhibiting xanthine oxidase and lipoxygenase activities with IC50 of 0.161 ± 0.111 and 0.018 ± 0.011 mg/mL, respectively. Trypsin hydrolysates of V. subterranea hydrolyzed for 5 h potently inhibited the activities of α-amylase and α-glucosidase with respective IC50 of 0.297 ± 0.060 and 0.314 ± 0.064 mg/mL. Overall, pepsin and trypsin hydrolysates of E. senegalensis demonstrated pronounced functional bioactivities relative to V. subterranea hydrolysates. This study concludes that both seeds could serve as unique matrices of potential functional bioactive peptides with prospects for managing diabetes.

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