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Novel Zn-Binding Peptide Isolated from Soy Protein Hydrolysates: Purification, Structure, and Digestion

Suyin ZhuSchool of Chemistry and Chemical Engineering, Guangzhou University, Guangzhou 510006, ChinaYing‐Min ZhengSchool of Chemistry and Chemical Engineering, Guangzhou University, Guangzhou 510006, ChinaShan HeFlinders Institute for NanoScale Science and Technology, College of Science and Engineering, Flinders University, Bedford Park, South Australia 5042, AustraliaDongxiao SuSchool of Chemistry and Chemical Engineering, Guangzhou University, Guangzhou 510006, ChinaAnindya NagSchool of Engineering, Macquarie University, Sydney 2109, AustraliaQingzhu ZengSchool of Chemistry and Chemical Engineering, Guangzhou University, Guangzhou 510006, ChinaYang YuanSchool of Chemistry and Chemical Engineering, Guangzhou University, Guangzhou 510006, China

2020en

ABI

Annotatsiya

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 ZnSO4 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.

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DOI: 10.1021/acs.jafc.0c05792

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