In this study, a novel Zn-binding peptide, Lys−Tyr−Lys−Arg−Gln−Arg−Trp (KYKRQRW), was purified and identified from soy protein isolate hydrolysates (SPIHs). The Zn-binding peptide exhibited improved Zn-binding capacity (83.21 ± 2.65%) than SPIH solutions. CD, NMR, and Fourier transform infrared spectroscopy were used to confirm the complexation between Zn and the peptide. The results showed that the Zn-binding peptide formed a folding structure with part of the β-sheet (29.3−13.4%) turning into random coils (41.7−57.6%) during complexation. It was further proved that the binding sites were located at the oxygen atoms on the carboxyl group of the Trp side chain and nitrogen atoms on the amino group of the Lys side chain. Moreover, the Zn−peptide complex exhibited increased solubility than ZnSO 4 during simulated gastrointestinal digestion. This study highlighted that the novel soy peptide possessed a strong zinc chelate rate and had a positive effect on the gastrointestinal stability of Zn which could be utilized as a functional ingredient in future.
BackgroundZinc is an essential trace element for the human body. Recently, a novel Zn-binding peptide, Lys-Tyr-Lys-Arg-Gln-Arg-Trp (PP), was purified and identified from soy protein hydrolysates with high Zn-binding capacity (83.21 ± 2.65%) by our previous study. The preparation of soy meal hydrolysates (SMHs)-Zn complexes is convenient and low-cost, while PP (Lys-Tyr-Lys-Arg-Gln-Arg-Trp)-Zn complexes have a higher coordination rate but a relatively high cost. The aim of this study was to investigate the effect of soy meal hydrolysates (SMHs)-Zn complexes on zinc absorption in mice model, and synthetic soy peptide (PP)-Zn complexes with high Zn-binding capacity were used as control. Firstly, SMHs were prepared by enzymolysis, and the PP (Lys-Tyr-Lys-Arg-Gln-Arg-Trp) were synthesized based on previous studies. The binding mechanism of soy hydrolysates and zinc was analyzed by spectral analysis. Furthermore, the cytotoxicity of the SMHs-Zn complexes was also studied using the CCK-8 method. The effect of zinc absorption was evaluated based on Zn content, total protein and albumin content, relevant enzyme system, and the PeT1 and ZnT1 mRNA expression levels.ResultThe result showed that zinc was bound with carboxyl oxygen and amino nitrogen atoms on SMHs, with hydrophobic and electrostatic interactions as auxiliary stabilizing forces. SMHs-Zn were proved to have great solubility and a small particle size at different pH values, and it showed a beneficial effect on Caco-2 cells growth. Moreover, it was proved that SMHs-Zn and PP-Zn could increase the levels of zinc and the activity of Zn-related enzymes in mice. SMHs-Zn possessed higher PepT1 and ZnT1 mRNA expression levels than PP-Zn in the small intestine.ConclusionSMHs-Zn with a lower Zn-binding capacity had similar effects on zinc absorption in mice as PP-Zn, suggesting that the bioavailability of peptide-zinc complexes in mice was not completely dependent on their Zn-binding capacity, but may also be related to the amino acid composition.
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