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(L.)M. Roem种子蛋白水解物的体外血管紧张素-1转换酶、α-淀粉酶和α-葡萄糖苷酶抑制及抗氧化活性

In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of (L.) M. Roem seed protein hydrolysate.

作者信息

Arise Rotimi Olusanya, Idi Jalil James, Mic-Braimoh Iseoluwa Maureen, Korode Emmanuel, Ahmed Risikat Nike, Osemwegie Omorefosa

机构信息

Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, Nigeria.

Department of Biological Sciences, College of Science and Engineering, Landmark University, Omu-Aran, Nigeria.

出版信息

Heliyon. 2019 May 7;5(5):e01634. doi: 10.1016/j.heliyon.2019.e01634. eCollection 2019 May.

Abstract

In recent times, researchers have explored food derived peptides to circumvent the side effects of synthetic drugs. This study therefore examined the amino acid constituents, antioxidant activities, angiotensin-1-converting enzyme (ACE), α-glucosidase and α-amylase inhibition kinetics of protein hydrolysate obtained from the seed of . The peptide yield by pepsin (16.93 ± 0.28%) and trypsin (13.20 ± 1.02%) were significantly lower than that of Alcalase (34.04 ± 1.96%). Alcalase hydrolysate however displayed the highest ferric reducing antioxidant capacity (FRAC), 1,1-diphenyl-2-picrylhydrazyl (DPPH) and HO scavenging activities (0.63%, 85.88% and 41.69% respectively), while the highest superoxide scavenging activity was shown by peptic hydrolysate (57.89%). The ACE inhibition by the hydrolysates with IC of 0.32-0.93 mg/mL, increased as the concentration of the peptic hydrolysate increased with the highest ACE-inhibitory activity (74.99 ± 0.43%) at 1.2 mg/mL of peptic hydrolysate. Tryptic and Alcalase hydrloysates exhibited a strong α-amylase inhibition having 27.96 ± 0.06% and 36.36 ± 0.71% inhibitory capacity respectively with IC of 1.02-3.31 mg/mL. Alcalase hydrolysates demonstrated the strongest inhibition (65.81 ± 1.95%), followed by tryptic hydrolysates (54.53 ± 0.52%) in a concentration-dependent inhibition of α-glucosidase (IC 0.48-0.80 mg/mL). Kinetic analysis showed that ACE-inhibition by different concentrations of Alcalase, pepsin and trypsin hydrolysates is uncompetitive, mixed-type and non-competitive respectively. α-Amylase was non-competitively inhibited while α-glucosidase was un-competitively inhibited by all the hydrolysates. The total amino acid concentration for Alcalase, trypsin and pepsin hydrolysates was 53.51g/100g, 75.40g/100g and 85.42g/100g of seed protein hydrolysate respectively, with glutamate being the most concentrated essential amino acid in all the three hydrolysates. From these results, it can be deduced that seed Alcalase and tryptic protein hydrolysates may play critical and indispensible role as bio-tools in diabetes and hypertension treatment.

摘要

近年来,研究人员探索了食物衍生肽以规避合成药物的副作用。因此,本研究检测了从[种子名称未给出]种子中获得的蛋白质水解物的氨基酸组成、抗氧化活性、血管紧张素 -1- 转换酶(ACE)、α - 葡萄糖苷酶和α - 淀粉酶抑制动力学。胃蛋白酶(16.93 ± 0.28%)和胰蛋白酶(13.20 ± 1.02%)的肽产率显著低于碱性蛋白酶(34.04 ± 1.96%)。然而,碱性蛋白酶水解物表现出最高的铁还原抗氧化能力(FRAC)、1,1 - 二苯基 -2- 苦基肼(DPPH)和羟基自由基清除活性(分别为0.63%、85.88%和41.69%),而胃蛋白酶水解物表现出最高的超氧阴离子清除活性(57.89%)。水解物对ACE的抑制作用,其IC50为0.32 - 0.93mg/mL,随着胃蛋白酶水解物浓度的增加而增强,在胃蛋白酶水解物浓度为1.2mg/mL时具有最高的ACE抑制活性(74.99 ± 0.43%)。胰蛋白酶和碱性蛋白酶水解物对α - 淀粉酶表现出较强的抑制作用,抑制能力分别为27.96 ± 0.06%和36.36 ± 0.71%,IC50为1.02 - 3.31mg/mL。在对α - 葡萄糖苷酶的浓度依赖性抑制中(IC50为0.48 - 0.80mg/mL),碱性蛋白酶水解物表现出最强的抑制作用(65.81 ± 1.95%),其次是胰蛋白酶水解物(54.53 ± 0.52%)。动力学分析表明,不同浓度的碱性蛋白酶、胃蛋白酶和胰蛋白酶水解物对ACE的抑制作用分别为非竞争性、混合型和竞争性。所有水解物对α - 淀粉酶均为非竞争性抑制,对α - 葡萄糖苷酶均为非竞争性抑制。碱性蛋白酶、胰蛋白酶和胃蛋白酶水解物中总氨基酸浓度分别为53.51g/100g、75.40g/100g和85.42g/100g的[种子名称未给出]种子蛋白水解物,谷氨酸是所有三种水解物中含量最高的必需氨基酸。从这些结果可以推断,[种子名称未给出]种子的碱性蛋白酶和胰蛋白酶蛋白水解物在糖尿病和高血压治疗中可能作为生物工具发挥关键且不可或缺的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4b17/6512875/9db6f2bc3d7c/gr1.jpg

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