References

• Ahmad, N., Sharma, S., Alam, M. K., Singh, V. N., Shamsi, S. F., Mehta, B. R., & Fatma, A. (2012). Rapid synthesis of silver nanoparticles using dried medicinal plant of Basil. Colloids and Surfaces B-Biointerfaces, 81(1), 81–86. https://doi.org/10.1016/j.colsurfb.2010.06.029
   Web of Science ®Google Scholar
• Akbar, B., Niloufar, N., Abolfazl, M., Lofollah, S., Ali, K. Q., & Soheyla, V. (2013). Evaluation and comparison of zinc absorption level from 2-alkyle 3-hydroxy pyranon-zinc complexes and zinc sulfate in rat in vivo. Advanced Biomedical Research, 2(1), 77. https://doi.org/10.4103/2277-9175.116432
   PubMedGoogle Scholar
• Armas, A., Sonois, V., Mothes, E., Mazarguil, H., & Faller, P. (2006). Zinc(II) binds to the neuroprotective peptide humanin. Journal of Inorganic Biochemistry, 100(10), 1672–1678. https://doi.org/10.1016/j.jinorgbio.2006.06.002
   PubMed Web of Science ®Google Scholar
• Bae, I. Y., Kim, H. Y., Lee, S., & Lee, H. G. (2011). Effect of the degree of oxidation on the physicochemical and biological properties of Grifola frondosa polysaccharides. Carbohydrate Polymers, 83(3), 1298–1302. https://doi.org/10.1016/j.carbpol.2010.09.037
   Web of Science ®Google Scholar
• Blindauer, C. A., Harvey, I., Bunyan, K. E., Stewart, A. J., Sleep, D., Harrison, D. J., Berezenko, S., & Sadler, P. (2009). Structure, properties, and engineering of the major zinc binding site on human albumin. Journal of Biological Chemistry, 284(34), 23116–23124. https://doi.org/10.1074/jbc.M109.003459
   PubMed Web of Science ®Google Scholar
• Chen, D., Liu, Z., Huang, W., Zhao, Y., Dong, S., & Zeng, M. (2013). Purification and characterisation of a zinc-binding peptide from oyster protein hydrolysate. Journal of Functional Foods, 5(2), 689–697. https://doi.org/10.1016/j.jff.2013.01.012
   Web of Science ®Google Scholar
• Dam, H., Kristensen, G., Nielsen, G. K., Prange, I., & Sondergaard, E. (1956). Influence of varied levels of peanut oil and cholesterol on cholesterol and polyenoic acids in tissues of the chicks. Acta physiologica, 36(4), 319–328. https://doi.org/10.1111/j.1748-1716.1956.tb01328.x
   Web of Science ®Google Scholar
• Depciuch, J., Sowa-Kućma, M., Nowak, G., Szewczyk, B., Doboszewska, U., & Parlinska-Wojtan, M. (2017). The role of zinc deficiency-induced changes in the phospholipid-protein balance of blood serum in animal depression model by Raman, FTIR and UV–vis spectroscopy. Biomedicine & Pharmacotherapy, 89(2017), 549–558. https://doi.org/10.1016/j.biopha.2017.01.180
   Web of Science ®Google Scholar
• Gerbino, E., Mobili, P., Tymczyszyn, E., Fausto, R., & Gómez-Zavaglia, A. (2011). FTIR spectroscopy structural analysis of the interaction between Lactobacillus kefir S-layers and metal ions. Journal of Molecular Structure, 987(1–3), 186–192. https://doi.org/10.1016/j.molstruc.2010.12.012
   Web of Science ®Google Scholar
• Guo, P., Qi, Y., Zhu, C., & Wang, Q. (2015). Purification and identification of antioxidant peptides from Chinese cherry (Prunus pseudocerasusLindl.) seeds. Journal of Functional Foods, 19(2015), 394–403. https://doi.org/10.1016/j.jff.2015.09.003
   Web of Science ®Google Scholar
• Hajji, L., Boukir, A., Assouik, J., Lakhiari, H., Kerbal, A., Doumenq, P., Mille, G., & Carvalho, M. L. D. (2015). Conservation of Moroccan manuscript papers aged 150, 200 and 800years. Analysis by infrared spectroscopy (ATR-FTIR), X-ray diffraction (XRD), and scanning electron microscopy energy dispersive spectrometry (SEM–EDS). Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 136(2015), 1038–1046. https://doi.org/10.1016/j.saa.2014.09.127
   Web of Science ®Google Scholar
• Hedberg, Y., Herting, G., & Wallinder, I. O. (2011). Risks of using membrane filtration for trace metal analysis and assessing the dissolved metal fraction of aqueous media – A study on zinc, copper and nickel. Environmental Pollution, 159(5), 1144–1150. https://doi.org/10.1016/j.envpol.2011.02.014
   PubMed Web of Science ®Google Scholar
• Huang, S. L., Zhao, L. N., Cai, X., Wang, S. Y., Huang, Y. F., Hong, J., & Rao, P. F. (2015). Purification and characterisation of a glutamic acid-containing peptide with calcium-binding capacity from whey protein hydrolysate. Journal of Dairy Research, 82(1), 29–35. https://doi.org/10.1017/s0022029914000715
   PubMed Web of Science ®Google Scholar
• Jin, Y. G., Fu, W. W., & Ma, M. H. (2011). Preparation and structure characterization of soluble bone collagen peptide chelating calcium. African Journal of Biotechnology, 10(50), 11. https://doi.org/10.5897/ajb10.1923
   Google Scholar
• Li, B., He, H., Shi, W., & Hou, T. (2019). Effect of duck egg white peptide-ferrous chelate on iron bioavailability in vivo and structure characterization. Journal of the Science of Food and Agriculture, 99(4), 1834–1841. https://doi.org/10.1002/jsfa.9377
   Google Scholar
• Liao, W., Lai, T., Chen, L., Fu, J., Sreenivasan, S. T., Yu, Z., & Ren, J. (2016). Synthesis and characterization of a walnut peptides–zinc complex and its antiproliferative activity against human breast carcinoma cells through the induction of apoptosis. Journal of Agricultural & Food Chemistry, 104(7), 849–859. https://doi.org/10.1021/acs.jafc.5b04924
   Google Scholar
• Makowska, J., Zamojc, K., Wyrzykowski, D., Uber, D., Wierzbicka, M., Wiczk, W., & Chmurzynski, L. (2016). Binding of Cu(II) ions to peptides studied by fluorescence spectroscopy and isothermal titration calorimetry. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 153(2016), 451–456. https://doi.org/10.1016/j.saa.2015.08.016
   Web of Science ®Google Scholar
• Miquel, E., & Farré, R. (2007). Effects and future trends of casein phosphopeptides on zinc bioavailability. Trends in Food Science & Technology, 18(3), 139–143. https://doi.org/10.1016/j.tifs.2006.11.004
   Web of Science ®Google Scholar
• Muyonga, J. H., Cole, C. G. B., & Duodu, K. G. (2004). Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chemistry, 85(1), 81–89. https://doi.org/10.1016/j.foodchem.2003.06.006
   Web of Science ®Google Scholar
• Nune, M., Krishnan, U. M., & Sethuraman, S. (2016). PLGA nanofibers blended with designer self-assembling peptides for peripheral neural regeneration. Materials Science and Engineering C-Materials for Biological Applications, 62(2016), 329–337. https://doi.org/10.1016/j.msec.2016.01.057
   Web of Science ®Google Scholar
• Oliveira, R. C., Hammer, P., Guibal, E., Taulemesse, J. M., & Garcia, O. (2014). Characterization of metal–biomass interactions in the lanthanum(III) biosorption on Sargassum sp. using SEM/EDX, FTIR, and XPS: Preliminary studies. Chemical Engineering Journal, 239(2014), 381–391. https://doi.org/10.1016/j.cej.2013.11.042
   Web of Science ®Google Scholar
• Predieri, G., Tegoni, M., Cinti, E., Leonardi, G., & Ferruzza, S. (2003). Metal chelates of 2-hydroxy-4-methylthiobutanoic acid in animal feeding: Preliminary investigations on stability and bioavailability. Journal of Inorganic Biochemistry, 95(2–3), 221–224. https://doi.org/10.1016/s0162-0134(03)00067-9
   PubMed Web of Science ®Google Scholar
• Qian, J. Y., Chen, W., Zhang, W. M., & Zhang, H. (2009). Adulteration identification of some fungal polysaccharides with SEM, XRD, IR and optical rotation: A primary approach. Carbohydrate Polymers, 78(3), 620–625. https://doi.org/10.1016/j.carbpol.2009.05.025
   Web of Science ®Google Scholar
• Storcksdieck, S., Bonsmann, G., & Hurrell, R. F. (2007). Iron‐binding properties, amino acid composition, and structure of muscle tissue peptides from in vitro digestion of different meat sources. Journal of Food Science, 72(1), S019–S029. https://doi.org/10.1111/j.1750-3841.2006.00229.x
   PubMed Web of Science ®Google Scholar
• Swain, J. H., Tabatabai, L. B., & Reddy, M. B. (2002). Histidine content of low-molecular-weight beef proteins influences nonheme iron bioavailability in Caco-2 cells. The Journal of Nutrition, 132(2), 245–251. https://doi.org/10.1093/jn/132.2.245
   PubMed Web of Science ®Google Scholar
• Taylor, P. G., Martínez-Torres, C., Romano, E. L., & Layrisse, M. (1986). The effect of cysteine-containing peptides released during meat digestion on iron absorption in humans. The American Journal of Clinical Nutrition, 3(1), 68–71. https://doi.org/10.1093/ajcn/43.1.68
   Google Scholar
• Udechukwu, M. C., Collins, S. A., & Udenigwe, C. C. (2016). Prospects of enhancing dietary zinc bioavailability with food-derived zinc-chelating peptides. Food & Function, 7(10), 4137. https://doi.org/10.1039/c6fo00706f
   PubMed Web of Science ®Google Scholar
• Uppal, R., Lakshmi, K. V., & Valentine, A. M. (2008). Isolation and characterization of the iron-binding properties of a primitive monolobal transferrin from Ciona intestinalis[J]. JBIC Journal of Biological Inorganic Chemistry, 13(6), 873–885. https://doi.org/10.1007/s00775-008-0375-6
   PubMed Web of Science ®Google Scholar
• Wang, C., Li, B., & Ao, J. (2012). Separation and identification of zinc-chelating peptides from sesame protein hydrolysate using IMAC-Zn2⁺ and LC-MS/MS. Food Chemistry, 134(2), 1231–1238. https://doi.org/10.1016/j.foodchem.2012.02.204
   PubMed Web of Science ®Google Scholar
• Wang, C., Wang, C., Li, B., & Li, H. (2014). Zn(II) chelating with peptides found in sesame protein hydrolysates: Identification of the binding sites of complexes. Food Chemistry, 165(2014), 594–602. https://doi.org/10.1016/j.foodchem.2014.05.146
   Web of Science ®Google Scholar
• Wang, S. Y., Zhu, B. B., Li, D. Z., Fu, X. Z., & Shi, L. (2012). Preparation and characterization of TIO2/SPI composite film. Materials Letters, 83(none), 42–45. https://doi.org/10.1016/j.matlet.2012.05.104
   Google Scholar
• Wang, X., Zhou, J., Tong, P. S., & Mao, X. Y. (2011). Zinc-binding capacity of yak casein hydrolysate and the zinc-releasing characteristics of casein hydrolysate-zinc complexes. Journal of Dairy Science, 94(6), 2731–2740. https://doi.org/10.3168/jds.2010-3900
   PubMed Web of Science ®Google Scholar
• Warren, F. J., Gidley, M. J., & Flanagan, B. M. (2015). Infrared spectroscopy as a tool to characterise starch ordered structure- a joint FTIR-ATR, NMR, XRD and DSC study. Carbohydrate Polymers, 139(2015), 35–42. https://doi.org/10.1016/j.carbpol.2015.11.066
   Web of Science ®Google Scholar
• Wu, H., Liu, Z., Zhao, Y., & Zeng, M. (2012). Enzymatic preparation and characterization of iron-chelating peptides from anchovy (Engraulis japonicus) muscle protein. Food Research International, 48(2), 435–441. https://doi.org/10.1016/j.foodres.2012.04.013
   Web of Science ®Google Scholar
• Xu, N., Ren, Z., Zhang, J., Song, X., Gao, Z., Jing, H., Li, S., Wang, S., & Jia, L. (2017). Antioxidant and anti-hyperlipidemic effects of mycelia zinc polysaccharides by Pleurotus eryngii var. tuoliensis. International Journal of Biological Macromolecules, 95(2017), 204–214. https://doi.org/10.1016/j.ijbiomac.2016.11.060
   Web of Science ®Google Scholar
• Yan, X., Ye, R., & Chen, Y. (2015). Blasting extrusion processing: The increase of soluble dietary fiber content and extraction of soluble-fiber polysaccharides from wheat bran. Food Chemistry, 180(2015), 106–115. https://doi.org/10.1016/j.foodchem.2015.01.127
   Web of Science ®Google Scholar
• Yan, Z., Wen, X., Kang, Y., & Chu, W. (2016). Intermolecular interactions of α-amino acids and glycyl dipeptides with the drug domiphen bromide in aqueous solutions analyzed by volumetric and UV–vis spectroscopy methods. The Journal of Chemical Thermodynamics, 101(2016), 300–307. https://doi.org/10.1016/j.jct.2016.06.018
   Web of Science ®Google Scholar
• Zhang, C., Gao, Z., Hu, C., Zhang, J., Sun, X., Rong, C., & Jia, L. (2017). Antioxidant, antibacterial and anti-aging activities of intracellular zinc polysaccharides from Grifola frondosa SH-05. International Journal of Biological Macromolecules, 95(2017), 778–787. https://doi.org/10.1016/j.ijbiomac.2016.12.003
   Web of Science ®Google Scholar
• Zhang, Y., Liu, J., Lu, X., Zhang, H., Wang, L., Guo, X., Qi, X., & Qian, H. (2013). Isolation and identification of an antioxidant peptide prepared from fermented peanut meal using fermentation. International Journal of Food Properties, 17(6), 1237–1253. https://doi.org/10.1080/10942912.2012.675605
   Web of Science ®Google Scholar
• Zhao, L., Cai, X., Huang, S., Wang, S., Huang, Y., Hong, J., & Rao, P. (2015). Isolation and identification of a whey protein-sourced calcium-binding tripeptide Tyr-Asp-Thr. International Dairy Journal, 40(2015), 16–23. https://doi.org/10.1016/j.idairyj.2014.08.013
   Web of Science ®Google Scholar
• Zhao, L., Huang, S., Cai, X., Hong, J., & Wang, S. (2014). A specific peptide with calcium chelating capacity isolated from whey protein hydrolysate. Journal of Functional Foods, 10(2014), 46–53. https://doi.org/10.1016/j.jff.2014.05.013
   Web of Science ®Google Scholar