Production of a novel black soldier fly larvae (Hermetia illucens) protein hydrolysate-zinc chelate: Characterization, chelation mechanism, and zinc solubility.

Authors

Minhui Luo, Cunwen Wang, Fang Yang, Chenyang Xie

Published in

Food chemistry. Volume 525. Issue Pt 4. Pages 150711. Aug 07, 2026. Epub Aug 07, 2026.

Abstract

Zinc (Zn) is an essential trace element for humans and animals, meanwhile, as a novel raw material, the low-molecular-weight black soldier fly leave (BL) peptide can bind to Zn efficiently. The present study prepared a novel BL protein hydrolysate-Zn (BLPH-Zn) chelate to develop multifunctional Zn supplements. Briefly, the composition of BLPH was first analysed and 198 peptides were identified, among which 37 exhibited high predicted bioactivity including angiotensin-converting enzyme (ACE) inhibitory, dipeptidyl peptidase IV (DPP-IV) inhibitory, and antioxidant properties. The Zn chelation rate of BLPH-Zn was 52.96 ± 2.05% at the peptide-to-Zn mass ratio of 6:1, and cytotoxicity assays confirmed the safety of the chelate at concentrations up to 0.5 mg/mL. Zn binding induced a conformational rearrangement of BLPH, involving carboxy, amino, amide, and sulfhydryl groups. Moreover, BLPH-Zn exhibited a balanced amino acid composition, excellent antioxidant activity, and improved Zn solubility. All these results indicate that the BLPH-Zn can serve as a safe and multifunctional Zn supplement in functional zinc supplement industry.

PMID:
42571734
Bibliographic data and abstract were imported from PubMed on 10 Aug 2026.

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