Martin Alain Mune Mune , Samuel René Minka , Thomas Henle
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引用次数: 58
摘要
分离蛋白经Alcalase、热溶酶和胰蛋白酶水解。Alcalase产生的BBPH具有最高的血管紧张素转换酶(ACE)抑制性能(IC50: 52 µg/mL)。Alcalase和thermolysin产生的水解液具有相似的二肽基肽酶- iv (DPP-IV)抑制活性(IC50: 1.73 mg/mL)，而胰蛋白酶产生的水解液抑制活性较低。BBPH还具有显著的2,2-二苯基-1-苦味酰肼自由基清除和铁螯合活性，对氧化应激具有保护作用。热溶素产生的BBPH生物活性肽对模拟胃肠消化(SGID)具有较好的抗性，而DPP-IV和ACE抑制性能显著降低。SGID后，Alcalase产生的BBPH中分子量在200-400 Da范围内的肽的分子量分布显著减少。LC-ESI-TOF-MS和硅质谱分析显示，热溶素产生的BBPH中存在具有ACE和DPP-IV抑制特性的潜在肽。
Investigation on antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activity of Bambara bean protein hydrolysates
Protein isolate was hydrolysed by Alcalase, thermolysin and trypsin. BBPH produced by Alcalase showed highest angiotensin-converting enzyme (ACE) inhibitory properties (IC50: 52 µg/mL). Hydrolysates produced by Alcalase and thermolysin exhibited similar dipeptidyl peptidase-IV (DPP-IV) inhibitory activity (IC50: 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.
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