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首页> 外文期刊>Journal of Functional Foods >The potential roles of Pinto bean (Phaseolus vulgaris cv. Pinto) bioactive peptides in regulating physiological functions: Protease activating, lipase inhibiting and bile acid binding activities
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The potential roles of Pinto bean (Phaseolus vulgaris cv. Pinto) bioactive peptides in regulating physiological functions: Protease activating, lipase inhibiting and bile acid binding activities

机译:Pinto Bean(Phaseolus Vulgaris Cv.pinto)生物活性肽在调节生理功能中的潜在作用:蛋白酶活化,脂肪酶抑制和胆汁酸结合活性

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The aim of the study was to explore the physiological effects of Pinto bean peptides (PBP) and their structure-activity relationships. Five pre-screened PBPs were investigated. The results showed that PBPs enhanced the protease activity ranging from 333 to 400%, and conversely, they inhibited lipase activity ranging from similar to 23 to similar to 87%. It was suggested that the binding of PBP to pepsin (i.e. Asp52, Tyr113 and Tyr114) resulted in a broad flap extension and enlarged the S-3 pocket, which made the active site more accessible, whereas, catalytic residues (i.e. Ser153 and His264) of lipase were found strongly bound to PBPs and preventing the enzyme from hydrolysing lipids. PBPs also shown their ability in binding bile acid ranging from similar to 18 to similar to 71% via hydrogen bonds to the C5-OH, C11-OH, C15-OH or C21-OH of cholic acid and deoxycholic acid. This study highlighted the effectiveness and mechanism of PBP in preventing obesity, hyperlipidaemia and hypercholesterolemia. (C) 2017 Elsevier Ltd. All rights reserved.
机译:该研究的目的是探讨番茄豆肽(PBP)及其结构 - 活性关系的生理效果。研究了五种预筛分的PBP。结果表明,PBPS增强了333至400%的蛋白酶活性,并相反,它们抑制了脂肪酶活性,范围与23类似于87%。有人建议,PBP对胃蛋白酶的结合(即ASP52,Tyr113和Tyr114)导致宽翼片延伸并扩大了S-3袋,使得活性位点更可易于易于获得,而催化残基(即Ser153和His264)发现脂肪酶强烈地与PBP结合并防止酶水解脂质。 PBPS还示出了它们在与氢键与胆酸和脱氧胆酸的C5-OH,C11-OH,C15-OH或C21-OH或C21-OH相似的胆汁酸的能力。该研究强调了PBP在预防肥胖,高脂血症和高胆固醇血症方面的有效性和机制。 (c)2017 Elsevier Ltd.保留所有权利。

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