竹豆蛋白水解物的抗氧化、血管紧张素转化酶和二肽基肽酶 IV 抑制活性的研究。
Investigation on antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activity of Bambara bean protein hydrolysates.
机构信息
Faculty of Science, University of Maroua, PO Box 814, Maroua, Cameroon.
Department of Biochemistry, University of Yaoundé I, PO Box 812, Yaoundé, Cameroon.
出版信息
Food Chem. 2018 Jun 1;250:162-169. doi: 10.1016/j.foodchem.2018.01.001. Epub 2018 Jan 2.
Protein isolate was hydrolysed by Alcalase, thermolysin and trypsin. BBPH produced by Alcalase showed highest angiotensin-converting enzyme (ACE) inhibitory properties (IC: 52 µg/mL). Hydrolysates produced by Alcalase and thermolysin exhibited similar dipeptidyl peptidase-IV (DPP-IV) inhibitory activity (IC: 1.73 mg/mL), while low inhibitory activity was observed for hydrolysate produced by trypsin. BBPH also showed protective effect against oxidative stress with significant 2,2-diphenyl-1-picrylhydrazyl radical scavenging and ferrous chelating activity. Bioactive peptides of BBPH produced by thermolysin showed better resistance to simulated gastrointestinal digestion (SGID), while the DPP-IV and ACE inhibitory properties were significantly reduced. Molecular weight distribution showed significant reduction in peptides of the molecular weight range 200-400 Da in BBPH produced by Alcalase, after SGID. LC-ESI-TOF-MS and in silico analysis showed the presence of potential peptides with both ACE and DPP-IV inhibitory properties in BBPH produced by thermolysin.
蛋白质分离物经 Alcalase、胰凝乳蛋白酶和胰蛋白酶水解。Alcalase 产生的 BBPH 表现出最高的血管紧张素转化酶（ACE）抑制特性（IC：52μg/mL）。Alcalase 和胰凝乳蛋白酶产生的水解产物表现出相似的二肽基肽酶-IV（DPP-IV）抑制活性（IC：1.73mg/mL），而胰蛋白酶产生的水解产物抑制活性较低。BBPH 还显示出对氧化应激的保护作用，具有显著的 2,2-二苯基-1-苦基肼自由基清除和亚铁螯合活性。由胰凝乳蛋白酶产生的 BBPH 的生物活性肽对模拟胃肠道消化（SGID）具有更好的抗性，而 DPP-IV 和 ACE 抑制特性则显著降低。分子量分布显示，经 SGID 处理后，Alcalase 产生的 BBPH 中 200-400Da 分子量范围内的肽显著减少。LC-ESI-TOF-MS 和计算机分析表明，在由胰凝乳蛋白酶产生的 BBPH 中存在具有 ACE 和 DPP-IV 抑制特性的潜在肽。
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