Corn distillers solubles by two-step proteolytic hydrolysis as a new source of plant-based protein hydrolysates with ACE and DPP4 inhibition activities

被引:23
作者
Sharma, Sonu [1 ]
Pradhan, Ranjan [1 ,2 ]
Manickavasagan, Annamalai [1 ]
Tsopmo, Apollinaire [3 ]
Thimmanagari, Mahendra [4 ]
Dutta, Animesh [1 ]
机构
[1] Univ Guelph, Sch Engn, Guelph, ON N1G 2W1, Canada
[2] Shrimp Canada, 67 Watson Rd S Unit 2, Guelph, ON N1L 1E3, Canada
[3] Carleton Univ, Dept Chem, Food Sci Program, 1125 Colonel Dr, Ottawa, ON K1S 5B6, Canada
[4] Ontario Minist Agr, Food & Rural Affairs, 1 Stone Rd West, Guelph, ON N1G 4Y1, Canada
关键词
Protein; Peptides; ACE; DPP4; Hydrolysate; DIPEPTIDYL-PEPTIDASE-IV; ANGIOTENSIN-CONVERTING ENZYME; BIOACTIVE PEPTIDES; ANTIOXIDANT; IDENTIFICATION; PURIFICATION; SOLUBILITY; ALCALASE;
D O I
10.1016/j.foodchem.2022.134120
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Proteins of low-value and underexplored corn distillers solubles (CDS) have not been considerably valorized. Hence, the influence of one-step enzymatic hydrolysis of proteins with alcalase (A), trypsin (T) or flavourzyme (F) and two steps with AT, TA, AF, FA, TF, or FT was assessed to release peptides with angiotensin-I converting enzyme inhibition (ACEi) and dipeptidyl peptidase4 inhibition (DPP4i). The AF hydrolysate was the best sample in terms of yield, protein content, degree of hydrolysis, ACEi (97.68 +/- 1.09 %), and DPP4i (51.51 +/- 0.28 %). Mass spectrometry of the most active AF hydrolysate (<3 kDa) identified new major peptides like APLA, PLFP, LFLP, LPPYL, PLYPLP, NDWHTGPL, LPPYLPS, GSPFLGQ, SWQQPIVGG. Bioinformatic analysis showed these can inhibit both ACE and DPP4. This is because peptides contain functional groups and adopt conformations significantly binding with other functional groups at enzyme active sites (p < 0.05). This establishes dual bioactivity of peptides, which may have applications in food, feed, and pharmaceutical industries.
引用
收藏
页数:17
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