Preparation of Saltiness-Enhancing Enzymatic Hydrolyzed Pea Protein and Identification of the Functional Small Peptides of Salt Reduction
Xue Xia, Shiqing Song, Tong Zhou, Han Zhang, Heping Cui, Foxin Zhang, Khizar Hayat, Xiaoming Zhang, Chi‐Tang Ho
Abstract
According to the correlation of saltiness determined by electronic tongue and perceived NaCl concentration, favorable enzymatic hydrolysis parameters were achieved to prepare the saltiness enhancing mixture peptides from pea protein. Six peptide fractions (F1, F2, F3, F4, F5, and F6) were isolated using Sephadex G-10 gel filtration. Among them, fraction F4 (0.1%) exhibited the highest saltiness (5.90 ± 0.03). The amino acid sequences of five main peptides identified by time-of-flight mass spectrometry were Tyr-Trp (367.40 Da), Gly-Glu-His-Glu (470.43 Da), Glu-Arg-Phe-Gly-Pro (604.65 Da), Gly-Ala-Gly-Lys (331.37 Da), and Pro-Gly-Ala-Gly-Asn (414.41 Da). Tyr-Trp (0.01%) in 0.4% NaCl solution had a 20% saltiness-enhancement compared with 0.4% NaCl solution. More salivary aldosterone was secreted after tasting hydrolysate or Tyr-Trp solutions via enzyme-linked immunosorbent assay, reflecting the improvement of human sensitivity to saltiness. Thereby, the saltiness-enhancing effect was confirmed for the small peptides from hydrolyzed pea protein and the main contributor was further identified.