Effect of Molecular Weight of Tilapia (Oreochromis Niloticus) Skin Collagen Peptide Fractions on Zinc-Chelating Capacity and Bioaccessibility of the Zinc-Peptide Fractions Complexes in Vitro Digestion
Source abstract
Abstract
To investigate the effect of the molecular weight of tilapia skin collagen peptide fractions on their zinc chelation capacity and the bioaccessibility of their zinc complexes, we evaluated the zinc-chelating ability of different molecular weight peptide, the solubility, and the stability of the complexes during simulated in vitro digestion. Low molecular weight peptide (P1) exhibited a higher zinc-chelating ability, which can be attributed to the variety of metal chelate amino acid residues. The highest solubility and the lowest release of zinc during peptic digestion for the P1-zinc complex and the zinc binding to P1 were retained at approximately 50% after peptic-pancreatic digestion. Fourier transform infrared spectroscopy indicated the primary involvement of the N-H group in all peptide-zinc complexes. This finding suggests that low molecular weight peptidefraction with strong zinc chelation ability can be used as delivery agents to improve zinc bioaccessibility.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Protein Hydrolysis and Bioactive Peptides · Meat and Animal Product Quality · Phytase and its Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Hainan Engineering Research Center of Aquatic Resources Efficient Utilization in South China Sea, Hainan University, Haikou 570228, Hainan, China
College of Food Science and Technology, Hainan University, Haikou 570228, Hainan, China
Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116000, Liaoning, China
References (38)
Show source-provided references
1. Nriagu, J. (2011). Zinc deficiency in human health. Encycl. Environ. Health, 789–800.10.1016/B978-0-444-52272-6.00674-7 ↗
2. Prospects of enhancing dietary zinc bioavailability with food-derived zinc-chelating peptides10.1039/C6FO00706F ↗
3. Human zinc deficiency10.1093/jn/130.5.1344S ↗
4. Discovery of human zinc deficiency: 50 years later10.1016/j.jtemb.2012.04.004 ↗
5. Zinc and its role in immunity and inflammation10.1016/j.autrev.2014.11.008 ↗
6. Evaluation and comparison of zinc absorption level from 2-alkyle 3-hydroxy pyranonzinc complexes and zinc sulfate in rat in vivo10.4103/2277-9175.116432 ↗
7. Food protein-derived chelating peptides: Biofunctional ingredients for dietary mineral bioavailability enhancement10.1016/j.tifs.2014.02.007 ↗
8. Zinc-binding capacity of yak casein hydrolysate and the zinc-releasing characteristics of casein hydrolysate-zinc complexes10.3168/jds.2010-3900 ↗
9. Purification and characterization of a zinc-binding peptide from oyster protein hydrolysate10.1016/j.jff.2013.01.012 ↗
10. Influence of structural and surface properties of whey-derived peptides on zinc-chelating capacity, and in vitro gastric stability and bioaccessibility of the zinc-peptide complexes10.1016/j.foodchem.2017.08.063 ↗
11. Fractionation and identification of alaska pollock skin collagen-derived mineral chelating peptides10.1016/j.foodchem.2014.10.055 ↗
12. Effect of soluble soybean protein hydrolysate-calcium complexes on calcium uptake by Caco-2 cells10.1111/j.1750-3841.2008.00873.x ↗
13. Separation and identification of zinc-chelating peptides from sesame protein hydrolysate using IMAC-Zn2+ and LC–MS/MS10.1016/j.foodchem.2012.02.204 ↗
14. Collagen peptides isolated from salmo salar and tilapia nilotica skin accelerate wound healing by altering cutaneous microbiome colonization via upregulated NOD2 and BD1410.1021/acs.jafc.9b08002 ↗
15. Particulate nanocomposite from oyster (Crassostrea rivularis) hydrolysates via zinc chelation improves zinc solubility and peptide activity10.1016/j.foodchem.2018.03.030 ↗
16. Metal solubility enhancing peptides derived from barley protein10.1016/j.foodchem.2014.03.061 ↗
17. Enzymatic hydrolysis kinetics and nitrogen recovery in the protein hydrolysate production from pig bones10.1016/j.jfoodeng.2013.06.040 ↗
18. Influence of average molecular weight on antioxidant and functional properties of cartilage collagen hydrolysates from Sphyrna lewini, Dasyatis akjei and Raja porosa10.1016/j.foodres.2012.12.031 ↗
19. Particle size distribution of rice flour affecting the starch enzymatic hydrolysis and hydration properties10.1016/j.carbpol.2013.06.002 ↗
20. Interfacial properties of tryptic peptides of b-lactoglobulin10.1021/jf00016a030 ↗
21. Influence of hydrolysis behaviour and microfluidisation on the functionality and structural properties of collagen hydrolysates10.1016/j.foodchem.2017.01.049 ↗
22. Characterization of structural and functional properties of fish protein hydrolysates from surimi processing by-products10.1016/j.foodchem.2013.11.089 ↗
23. Contributions of molecular size, charge distribution, and specific amino acids to the iron-binding capacity of sea cucumber (Stichopus japonicus) ovum hydrolysates10.1016/j.foodchem.2017.03.077 ↗
24. Antioxidant activity of proteins and peptides10.1080/10408390701425615 ↗
25. Complexation of Al(III) with reduced glutathione in acidic aqueous solutions10.1016/j.jinorgbio.2008.11.007 ↗
26. Chemical and biological aspects of Cu2+ interactions with peptides and aminoglycosides10.1016/j.ccr.2005.04.027 ↗
27. Specific structure-stability relations in metallopeptides10.1016/S0010-8545(98)00261-6 ↗
28. Affinity purification and characterisation of chelating peptides from chickpea protein hydrolysates10.1016/j.foodchem.2011.04.103 ↗
29. Synthesis and characterization of mixed ligand complex of Zn (II) and Co (II) with amino acids: Relevance to zinc binding sites in zinc fingers10.1007/BF02709293 ↗
30. Comparison of characteristics and fibril-forming ability of skin collagen from barramundi (Lates calcarifer) and tilapia (Oreochromis niloticus)10.1016/j.ijbiomac.2017.09.022 ↗
31. Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes10.1016/j.jff.2018.08.019 ↗
32. FTIR spectra of whey and casein hydrolysates in relation to their functional properties10.1021/jf020387k ↗
33. Changes in the secondary structure of bovine casein by fourier transform infrared spectroscopy: Effects of calcium and temperature110.3168/jds.S0022-0302(98)75881-3 ↗
34. The preservative potential of octopus scraps peptides−zinc chelate against staphylococcus aureus: Its fabrication, antibacterial activity and action mode10.1016/j.foodcont.2018.11.015 ↗
35. Infrared spectroscopy of proteins10.1016/j.bbabio.2007.06.004 ↗
36. Effects and future trends of casein phosphopeptides on zinc bioavailability10.1016/j.tifs.2006.11.004 ↗
37. The effect of molecular weights on the survivability of caseinderived antioxidant peptides after the simulated gastrointestinal digestion10.1016/j.ifset.2012.07.009 ↗
38. Degradation and antioxidant activities of peptides and zinc–peptide complexes during in vitro gastrointestinal digestion10.1016/j.foodchem.2014.10.066 ↗