Preparation and flavor analysis of pea salty peptide by alkaline protease

  • ZHANG Hongli ,
  • FU Tianxin ,
  • JIANG Peng ,
  • QIU Ying ,
  • DIAO Jingjing ,
  • WANG Changyuan
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  • 1(College of Food Science, Heilongjiang Bayi Agricultural University, Daqing 163319, China)
    2(National Coarse Cereals Engineering Research Center, Daqing 163319, China)
    3(Heilongjiang Coarse Grain Processing and Quality Safety Engineering Technology Research Center, Daqing 163319, China)

Received date: 2025-08-20

  Revised date: 2025-11-21

  Online published: 2026-08-21

Abstract

This study produced salty peptides from pea protein using alkaline protease, flavor protease, trypsin, and papain.Optimization of the preparation process identified alkaline protease as the most effective enzyme.Qualitative and quantitative analysis of the hydrolysate's flavor profile and taste compounds identified the key peptide sequences and flavor-active amino acids. The ideal hydrolysis conditions were:enzyme dosage 3%, substrate concentration 0.075 g/mL, and hydrolysis time 4 h.Flavor analysis revealed that the <1 kDa hydrolysate fraction exhibited the strongest salty taste.BIOPEP-UWM screening identified a novel putative salty peptide, PGLAR (Pro-Gly-Leu-Ala-Arg, 512 Da).Molecular docking with the ENaC protein indicated a binding energy of -6.519 kcal/mol between PGLAR and the ENaC-α subunit.The peptide formed hydrophobic interactions with five residues (Pro437, Tyr407, Leu260, Leu263, Tyr140) and hydrogen bonds with four active sites (Tyr444, His298, Thr266, Pro264).Quantitative analysis identified glutamic acid and arginine as key contributors to the savory flavor.These findings offered technical and theoretical support for developing low-sodium foods and savory flavorings.

Cite this article

ZHANG Hongli , FU Tianxin , JIANG Peng , QIU Ying , DIAO Jingjing , WANG Changyuan . Preparation and flavor analysis of pea salty peptide by alkaline protease[J]. Food and Fermentation Industries, 2026 , 52(14) : 174 -183 . DOI: 10.13995/j.cnki.11-1802/ts.044238

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