Amiri ZR, Safari R, Bakhshandeh T, vavsari FA (2016) Functional properties of fish protein hydrolysates from Cuttlefish (Sepia pharaonis) muscle produced by two commercial enzymes. Iran J Fish Sci 15(4):1485-1499.
AOAC (2000) AOAC: Official Methods of Analysis. The Association of Official Analytical Chemists, USA.
Bouhallab S, Cinga V, Aiät-Oukhatar N, Bureau F, Neuville D et al (2002) Influence of various phosphopeptides of caseins on iron absorption. J Agric Food Chem 50(24):7127−7130. https://doi.org/10.1021/jf025554v
Bronner F, Pansu D (1999) Nutritional aspects of calcium absorption. J Nutr 129(1):9–12.
Caetano-Silva ME, Cilla A, Bertoldo-Pacheco MT, Netto FM, Alegría A (2018) Evaluation of in vitro iron bioavailability in free form and as whey peptide-iron complexes. J Food Compost Anal. 68:95-100. https://doi.org/10.1016/j.jfca.2017.03.010
Chalamaiah M, Kumar BD, Hemalatha R, Jyothirmayi T (2012) Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications: A review. Food Chem 135(4):3020–3038. https://doi.org/10.1016/j.foodchem.2012.06.100
Charoenphun N, Cheirsilp B, Sirinupong N, Youravong W (2013) Calcium-binding peptides derived from tilapia (Oreochromis niloticus) protein hydrolysate. Eur Food Res Technol 236(1):57–63. https://doi.org/10.1007/s00217-012-1860-2
Chen D, Mu X, Huang H, Nie R, Liu Z et al (2014) Isolation of a calcium-binding peptide from tilapia scale protein hydrolysate and its calcium bioavailability in rats. J Funct Foods 6:575-584. https://doi.org/10.1016/j.jff.2013.12.001
Cumby N, Zhong Y, Naczk M, Shahidi F (2008) Antioxidant activity and water-holding capacity of canola protein hydrolysates. Food Chem 109(1):144–148. https://doi.org/10.1016/j.foodchem.2007.12.039
Eckert E, Lu L, Unsworth LD, Chen L, Xie J et al (2016) Biophysical and in vitro absorption studies of iron chelating peptide from barley proteins. J Funct Foods 25:291-301. https://doi.org/10.1016/j.jff.2016.06.011
Foh MBK, Kamara MT, Amadou I, Foh BM, Wenshui X (2011) Chemical and physicochemical properties of tilapia (Oreochromis niloticus) fish protein hydrolysate and concentrate. Int J Biol Chem 5(1):21-36. http://dx.doi.org/10.3923/ijbc.2011.21.36
Gaucheron F (2000) Iron fortification in dairy industry. Trends Food Sci Technol 11(11):403–409. https://doi.org/10.1016/S0924-2244(01)00032-2
Gbogouri GA, Linder M, Fanni J, Parmentier M (2004) Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. J Food Sci 69(8):615–622. https://doi.org/10.1111/j.1365-2621.2004.tb09909.x
Guo L, Harnedy PA, Li B, Hou H, Zhang Z et al (2014) Food protein-derived chelating peptides: Biofunctional ingredients for dietary mineral bioavailability enhancement. Trends Food Sci Tech 37(2):92-105.
Guo L, Hou H, Li B, Zhang Z, Wang S et al (2013) Preparation, isolation and identification of iron-chelating peptides derived from Alaska pollock skin. Process Biochem 48(5-6):988–993. https://doi.org/10.1016/j.procbio.2013.04.013
Hershko C (2005) Treating iron overload: The state of the art. Semin Hematol. 42(2):S2-4. https://doi.org/10.1053/j.seminhematol.2005.01.003
Hou H, Wang S, Zhu X, Li Q, Fan Y et al (2018) A novel calcium-binding peptide from Antarctic krill protein hydrolysates and identification of binding sites of calcium-peptide complex. Food Chem 243:389-395.
Huang G, Ren L, Jiang J (2011a) Purification of a histidine-containing peptide with calcium binding activity from shrimp processing byproducts hydrolysate. Eur Food Res Technol 232(2):281–287. https://doi.org/10.1007/s00217-010-1388-2
Huang G, Ren Z, Jiang J (2011b) Separation of iron-binding peptides from shrimp processing by-products hydrolysates. Food Bioprocess Tech 4:1527–1532. https://doi.org/10.1007/s11947-010-0416-3
Inoue H, Ohira T, Ozaki N, Nagasawa H (2004) A novel calcium-binding peptide from the cuticle of the crayfish, Procambarus clarkii. Biochem Biophys Res Commun 318:649–654.
Intarasirisawat R, Benjakul S, Visessanguan W, Wu J (2012) Antioxidative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe. Food Chem 135(4):3039–3048. https://doi.org/10.1016/j.foodchem.2012.06.076
Jung WK, Kim SK (2007) Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame. Eur Food Res Technol 224(6):763–767. https://doi.org/10.1007/s00217-006-0371-4
Kang PY, Ishak NH, Sarbon NM (2018) Optimization of enzymatic hydrolysis of shortfin scad (Decapterus macrosoma) myofibrillar protein with antioxidant effect using alcalase. Int Food Res J 25(5):1808-1817.
Kristinsson HG, Rasco BA (2000) Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J Agric Food Chem 48(3):657−666. https://doi.org/10.1021/jf990447v
Ktari N, Jridi M, Bkhairia I, Sayari N, Salah RB et al (2012) Functionalities and antioxidant properties of protein hydrolysates from muscle of zebra blenny (Salaria basilisca) obtained with different crude protease extracts. Food Res Int 49(2):747–756. https://doi.org/10.1016/j.foodres.2012.09.024
Latorres JM, Rios DG, Saggiomo G, Jr. WW, Prentice-Hernandez C (2018) Functional and antioxidant properties of protein hydrolysates obtained from white shrimp (Litopenaeus vannamei). J Food Sci Technol 55(2):721–729. https://doi.org/10.1007/s13197-017-2983-z
Lee SH, Song KB (2009a) Isolation of a calcium-binding peptide from enzymatic hydrolysates of porcine blood plasma protein. J Korean Soc Appl Bi. 52(3):290-294.
Lee SH, Song KB (2009b) Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein. Process Biochem 44(3):378–381. https://doi.org/10.1016/j.procbio.2008.12.001
Li X, Luo Y, Shen H, You J (2012) Antioxidant activities and functional properties of grass carp (Ctenopharyngodon idellus) protein hydrolysates. J Sci Food Agric 92(2):292–298. https://doi.org/10.1002/jsfa.4574
Li Z, Wang B, Chi C, Gong Y, Luo H et al (2013) Influence of average molecular weight on antioxidant and functional properties of cartilage collagen hydrolysates from Sphyrna lewini, Dasyatis akjei and Raja porosa. Food Res Int 51(1):283–293. https://doi.org/10.1016/j.foodres.2012.12.031
Liu F-R, Wang L, Wang R, Chen Z-X (2013) Calcium-binding capacity of wheat germ protein hydrolysate and characterization of peptide-calcium complex. J Agric Food Chem 61(31):7537–7544.
Liu Q, Kong B, Xiong YL, Xia X (2010) Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis. Food Chem 118(2): 403–410. https://doi.org/10.1016/j.foodchem.2009.05.013
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193(1):265–275.
Naqash SY, Nazeer RA (2013) Antioxidant and functional properties of protein hydrolysates from pink perch (Nemipterus japonicus) muscle. J Food Sci Technol 50(5):972–978. https://doi.org/10.1007/s13197-011-0416-y
Nielsen PM, Petersen D, Dambmann C (2001) Improved method for determining food protein degree of hydrolysis. J Food Sci 66(5):642-646. https://doi.org/10.1111/j.1365-2621.2001.tb04614.x
Noman A, Xu Y, AL-Bukhaiti WQ, Abed SM, Ali AH et al (2018) Influence of enzymatic hydrolysis conditions on the degree of hydrolysis and functional properties of protein hydrolysate obtained from Chinese sturgeon (Acipenser sinensis) by using papain enzyme. Process Biochem 67:19-28. https://doi.org/10.1016/j.procbio.2018.01.009
Nourmohammadi E, SadeghiMahoonak A, Alami M, Ghorbani M (2017) Amino acid composition and antioxidative properties of hydrolysed pumpkin (Cucurbita pepo L.) oil cake protein. Int J Food Prop 20(12):3244-3255. https://doi.org/10.1080/10942912.2017.1283516
Nurdiani R, Dissanayake M, Street WE, Donkor ON, Singh TK et al (2016) In vitro study of selected physiological and physicochemical properties of fish protein hydrolysates from 4 Australian fish species. Int Food Res J 23(5):2029-2040.
Pacheco-Aguilar R, Mazorra-Manzano MA, Ramírez-Suárez JC (2008) Functional properties of fish protein hydrolysates from Pacific whiting (Merluccius productus) muscle produced by a commercial protease. Food Chem 109:782–789. https://doi.org/10.1016/j.foodchem.2008.01.047
Peng Z, Hou H, Zhang K, Li B (2017) Effect of calcium-binding peptide from pacific cod (Gadus macrocephalus) bone on calcium bioavailability in rats. Food Chem 221:373-378.
Putra SNKM, Ishak NH, Sarbon NM (2018) Preparation and characterization of physicochemical properties of golden apple snail (Pomacea canaliculata) protein hydrolysate as affected by different proteases. Biocatal Agric Biotechnol 13:123-128. https://doi.org/10.1016/j.bcab.2017.12.002
Santos SDAd, Martins VG, Salas-Mellado M, Prentice C (2011) Evaluation of functional properties in protein hydrolysates from bluewing searobin (Prionotus punctatus) obtained with different microbial enzymes. Food Bioprocess Technol 4(8):1399–1406. https://doi.org/10.1007/s11947-009-0301-0
Shu G, Zhang B, Zhang Q, Wan H, Li H (2017) Effect of temperature, pH, enzyme to substrate ratio, substrate concentration and time on the antioxidative activity of hydrolysates from goat milk casein by Alcalase. Acta Universitatis Cibiniensis. Series E: Food Technology 20(2):29-38. https://doi.org/10.1515/aucft-2016-0013
Souissi N, Bougatef A, Triki-Ellouz Y, Nasri M (2007) Biochemical and functional properties of sardinella (Sardinella aurita) by-product hydrolysates. Food Technol Biotech 45(2):187–194.
Sun N, Cui P, Jin Z, Wu H, Wang Y et al (2017) Contributions of molecular size, charge distribution, and specific amino acids to the iron-binding capacity of sea cucumber (Stichopus japonicus) ovum hydrolysates. Food Chem 230:627-636. https://doi.org/10.1016/j.foodchem.2017.03.077
Sun N, Wu H, Du M, Tang Y, Liu H et al (2016) Food protein-derived calcium chelating peptides: A review. Trends Food Sci Technol 58:140-148.
Thiansilakul Y, Benjakul S, Shahidi F (2007) Compositions, functional properties and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi). Food Chem 103(4):1385–1394. https://doi.org/10.1016/j.foodchem.2006.10.055
Vo TDL, Pham KT, Ha DQ (2018a) Recovery of proteolysate from salmon by-product: Investigation of antioxidant activity, optimization of hydrolysis, determination of iron-binding activity and identification of bioactive peptides. The International Journal of Engineering and Science 7(9):18-30. https://doi.org/10.9790/1813-0709041830
Vo TDL, Pham KT, Le LT, Nguyen TTH (2018b) Identification of a new calcium‐binding peptide from enzymatic proteolysate of Acetes japonicus. J Food Process Pres 42(12):e13837. https://doi.org/10.1111/jfpp.13837
Vo TDL, Pham KT, Le VMV, Lam HH, Huynh ON et al (2020) Evaluation of iron-binding capacity, amino acid composition, functional properties of Acetes japonicus proteolysate and identification of iron-binding peptides. Process Biochem 91:374-386. https://doi.org/10.1016/j.procbio.2020.01.007
Wang L, Ding Y, Zhang X, Li Y, Wang R et al (2018) Isolation of a novel calcium-binding peptide from wheat germ protein hydrolysates and the prediction for its mechanism of combination. Food Chem 239:416–426.
Wu H, Liu Z, Zhao Y, Zeng M (2012) Enzymatic preparation and characterization of iron-chelating peptides from anchovy (Engraulis japonicus) muscle protein. Food Res Int 48:435–441. https://doi.org/10.1016/j.foodres.2012.04.013
Wu R, Chen L, Liu D, Huang J, Zhang J et al (2017) Preparation of antioxidant peptides from salmon byproducts with bacterial extracellular proteases. Mar Drugs 15(4):1-19. https://dx.doi.org/10.3390%2Fmd15010004
Wu W, Li B, Hou H, Zhang H, Zhao X (2017) Identification of iron-chelating peptides from Pacific cod skin gelatin and the possible binding mode. J Funct Foods 35:418–427. https://doi.org/10.1016/j.jff.2017.06.013
Ying L, Kaihua W, Xiaoguang M, Yajuan W, Tuo Z et al (2017) Separation and identification of iron-chelating peptides from defatted walnut flake by NanoLC-ESI-MS/MS and De novo sequencing. Process Biochem 59B:223-228. https://doi.org/10.1016/j.procbio.2017.05.010
Yu Y, Fan F, Wu D, Yu C, Wang Z et al (2018) Antioxidant and ACE inhibitory activity of enzymatic hydrolysates from Ruditapes philippinarum. Molecules 23(5):E1189. https://dx.doi.org/10.3390%2Fmolecules23051189
Zayas JF (1997) Functionality of Proteins in Food. Springer, Germany.