Pentapeptide-Zinc Chelate from Sweet Almond Expeller Amandin Hydrolysates: Structural and Physicochemical Characteristics, Stability and Zinc Transport Ability In Vitro

Abstract

To promote the application of almond expellers, sweet almond expeller globulin (amandin) was extracted for the preparation of bioactive peptides. After dual enzymatic hydrolysis, Sephadex G-15 gel isolation, reverse-phase high-performance liquid chromatography purification and ESI-MS/MS analysis, two novel peptides Val-Asp-Leu-Val-Ala-Glu-Val-Pro-Arg-Gly-Leu (1164.45 Da) and Leu-Asp-Arg-Leu-Glu (644.77 Da) were identified in sweet almond expeller amandin hydrolysates. Leu-Asp-Arg-Leu-Glu (LDRLE) of excellent zinc-chelating capacity (24.73 mg/g) was selected for preparation of peptide-zinc chelate. Structural analysis revealed that zinc ions were mainly bonded to amino group and carboxyl group of LDRLE. Potential toxicity and some physicochemical properties of LDRLE and Val-Asp-Leu-Val-Ala-Glu-Val-Pro-Arg-Gly-Leu (VDLVAEVPRGL) were predicted in silico. The results demonstrated that both LDRLE and VDLVAEVPRGL were not toxic. Additionally, zinc solubility of LDRLE-zinc chelate was much higher than that of zinc sulphate and zinc gluconate at pH 6.0–10.0 and against gastrointestinal digestion at 37 °C (p < 0.05). However, incubation at 100 °C for 20–60 min significantly reduced zinc-solubility of LDRLE-zinc chelate. Moreover, the chelate showed higher zinc transport ability in vitro than zinc sulphate and zinc gluconate (p < 0.05). Therefore, peptides isolated from sweet almond expeller amandin have potential applications as ingredient of zinc supplements.