Abstract
The aims of this study included evaluation of copper-binding capacity (CBC) and amino acid composition of salmon by-product proteolysate and its peptide fractions, optimization of hydrolysis condition, and identification of copper-binding peptides from the proteolysate. The result was that under the ideal hydrolysis (Neutrase, temperature of 45 °C, pH 7, enzyme:substrate (E:S) proportion of 72.24 U/g protein and hydrolysis time of 8.02 h), the proteolysate had the indispensable amino acid content at approximately 38.7% and also displayed the maximal CBC of 15163.6 µg Cu2+/g protein. Besides, four peptide fractions of 10–30 kDa, 3–10 kDa, 1–3 kDa, and <1 kDa were recovered using ultrafiltration, among which the <1 kDa fraction had the highest CBC of 10852.00 ± 895.06 µgCu2+/g protein. A copper-binding peptide, Phe-Ile-Asp-Asp-Asp-Ala-Phe-Ile-Arg (1110 Da), was identified from this fraction using tandem mass spectrometry (MS/MS). As a whole, the proteolysate/peptides could be used for copper enhancement that could shield human body from copper inadequacy disorders.
Funding source: Vietnam National University HoChiMinh City (VNU–HCM)
Award Identifier / Grant number: C2017–20–34
Abbreviations and Nomenclature
- ANOVA
Analysis of variance
- AOAC
Association of Official Agricultural Chemists
- CBC
Copper-binding capacity
- DH
Degree of hydrolysis
- ddMS2
data-dependent second mass spectrometry
- E:S ratio
Enzyme:substrate ratio
- LDL
Low-density lipoprotein
- MS/MS
Tandem mass spectrometry or Mass spectrometry/mass spectrometry
- Na2EDTA
Disodium ethylenediaminetetraacetate
- RSM
Response surface methodology
Author contribution: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
Research funding: This research is funded by Vietnam National University HoChiMinh City (VNU–HCM) under grant number C2017–20–34.
Employment or leadership: None declared.
Honorarium: None declared.
Conflict of interest statement: The authors declare no conflicts of interest regarding this article.
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