Sharma Sonu, Pradhan Ranjan, Manickavasagan Annamalai, Thimmanagari Mahendra, Dutta Animesh
School of Engineering, University of Guelph, Guelph, ON N1G 2W1, Canada.
School of Engineering, University of Guelph, Guelph, ON N1G 2W1, Canada; Shrimp Canada, 67 Watson Rd. S (Unit - 2), Guelph, ON N1L 1 E3, Canada.
Food Chem. 2022 Sep 15;388:133036. doi: 10.1016/j.foodchem.2022.133036. Epub 2022 Apr 21.
Plant-based protein concentrate (PC) was extracted from under-utilized corn distillers solubles comprising a distinctive heat-treated blend of corn and yeast proteins. Enzymolysis of PC with alcalase generated protein hydrolysate (PH) containing angiotensin converting enzyme (ACE) inhibitory peptides. A novel kinetic model is developed to elucidate enzymolysis kinetics of PC. The PH of greatest DH (∼25%) revealed maximum ACE inhibition (%). Fractionated PH (<3 kDa) had non-toxic and non-allergenic unique peptides encrypted with anti-ACE fragments. Promising bioactive peptides (PeptideRanker > 0.85) docked with ACE had free energies between -8.40 and -10.60 kcal.mol greater than captopril (-6.34 kcal.mol). The yeast-derived RLLPF peptide interacted with all active pockets of ACE (S1, S2, S') via hydrogen-, polar- and hydrophobic-bonds. Docking results suggested that ARG, VAL, TRP, TYR, GLU, ALA, ARG, HIS, HIS, ASN, and ALA of ACE aided in stabilizing complexes with peptides. Thus, PH could be used as antihypertensive ingredient for feed, food, or pharmaceutical industries.
植物性浓缩蛋白（PC）是从未充分利用的玉米酒糟中提取的，它是玉米和酵母蛋白经过特殊热处理后的混合物。用碱性蛋白酶对PC进行酶解产生了含有血管紧张素转换酶（ACE）抑制肽的蛋白水解物（PH）。建立了一个新的动力学模型来阐明PC的酶解动力学。水解度（DH）最大（约25%）的PH显示出最大的ACE抑制率。分级后的PH（<3 kDa）含有用抗ACE片段编码的无毒且无致敏性的独特肽段。与ACE对接的有前景的生物活性肽（PeptideRanker>0.85）的自由能在-8.40至-10.60 kcal·mol之间，大于卡托普利（-6.34 kcal·mol）。酵母衍生的RLLPF肽通过氢键、极性键和疏水键与ACE的所有活性口袋（S1、S2、S'）相互作用。对接结果表明，ACE的ARG、VAL、TRP、TYR、GLU、ALA、ARG、HIS、HIS、ASN和ALA有助于稳定与肽的复合物。因此，PH可作为饲料、食品或制药行业的抗高血压成分。
