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Volumn 230, Issue , 2017, Pages 627-636

Contributions of molecular size, charge distribution, and specific amino acids to the iron-binding capacity of sea cucumber (Stichopus japonicus) ovum hydrolysates

Author keywords

Amino acids; Characterization; Iron binding; Molecular size; Sea cucumber ovum

Indexed keywords

AMINO ACIDS; BINDING SITES; BINS; CHARACTERIZATION; CHARGE DISTRIBUTION; CRYSTAL STRUCTURE; HYDROLYSIS; IRON; NITROGEN;

EID: 85016002026     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.03.077     Document Type: Article
Times cited : (131)

References (40)
  • 1
    • 0030586806 scopus 로고    scopus 로고
    • Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity
    • Adamson, N.J., Reynolds, E.C., Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity. Enzyme and Microbial Technology 19:3 (1996), 202–207.
    • (1996) Enzyme and Microbial Technology , vol.19 , Issue.3 , pp. 202-207
    • Adamson, N.J.1    Reynolds, E.C.2
  • 2
    • 0003737812 scopus 로고
    • Enzymic hydrolysis of food proteins
    • Elsevier Applied Science Publishers
    • Adler-Nissen, J., Enzymic hydrolysis of food proteins. 1986, Elsevier Applied Science Publishers.
    • (1986)
    • Adler-Nissen, J.1
  • 3
    • 79953082035 scopus 로고    scopus 로고
    • Reducing, radical scavenging, and chelation properties of fermented soy protein meal hydrolysate by Lactobacillus plantarum LP6
    • Amadou, I., Le, G.W., Shi, Y.H., Jin, S., Reducing, radical scavenging, and chelation properties of fermented soy protein meal hydrolysate by Lactobacillus plantarum LP6. International Journal of Food Properties 14:3 (2011), 654–665.
    • (2011) International Journal of Food Properties , vol.14 , Issue.3 , pp. 654-665
    • Amadou, I.1    Le, G.W.2    Shi, Y.H.3    Jin, S.4
  • 6
    • 84925203406 scopus 로고    scopus 로고
    • Iron-binding peptides from whey protein hydrolysates: Evaluation, isolation and sequencing by LC–MS/MS
    • Caetano-Silva, M.E., Bertoldo-Pacheco, M.T., Paes-Leme, A.F., Netto, F.M., Iron-binding peptides from whey protein hydrolysates: Evaluation, isolation and sequencing by LC–MS/MS. Food Research International 71 (2015), 132–139.
    • (2015) Food Research International , vol.71 , pp. 132-139
    • Caetano-Silva, M.E.1    Bertoldo-Pacheco, M.T.2    Paes-Leme, A.F.3    Netto, F.M.4
  • 9
    • 84876731664 scopus 로고    scopus 로고
    • Purification and characterisation of a zinc-binding peptide from oyster protein hydrolysate
    • Chen, D., Liu, Z., Huang, W., Zhao, Y., Dong, S., Zeng, M., Purification and characterisation of a zinc-binding peptide from oyster protein hydrolysate. Journal of Functional Foods 5:2 (2013), 689–697.
    • (2013) Journal of Functional Foods , vol.5 , Issue.2 , pp. 689-697
    • Chen, D.1    Liu, Z.2    Huang, W.3    Zhao, Y.4    Dong, S.5    Zeng, M.6
  • 10
    • 0030899892 scopus 로고    scopus 로고
    • Iron uptake is enhanced in Caco-2 cell monolayers by cysteine and reduced cysteinyl glycine
    • Glahn, R.P., Van Campen, D.R., Iron uptake is enhanced in Caco-2 cell monolayers by cysteine and reduced cysteinyl glycine. The Journal of Nutrition 127:4 (1997), 642–647.
    • (1997) The Journal of Nutrition , vol.127 , Issue.4 , pp. 642-647
    • Glahn, R.P.1    Van Campen, D.R.2
  • 11
    • 80053568380 scopus 로고    scopus 로고
    • Separation of iron-binding peptides from shrimp processing by-products hydrolysates
    • Huang, G., Ren, Z., Jiang, J., Separation of iron-binding peptides from shrimp processing by-products hydrolysates. Food and Bioprocess Technology 4:8 (2011), 1527–1532.
    • (2011) Food and Bioprocess Technology , vol.4 , Issue.8 , pp. 1527-1532
    • Huang, G.1    Ren, Z.2    Jiang, J.3
  • 12
    • 77951960886 scopus 로고    scopus 로고
    • Iron bioavailability and dietary reference values
    • Hurrell, R., Egli, I., Iron bioavailability and dietary reference values. The American Journal of Clinical Nutrition 91:5 (2010), 1461S–1467S.
    • (2010) The American Journal of Clinical Nutrition , vol.91 , Issue.5 , pp. 1461S-1467S
    • Hurrell, R.1    Egli, I.2
  • 13
    • 84995783173 scopus 로고    scopus 로고
    • Effect of structure changes on hydrolysis degree, moisture state, and thermal denaturation of egg white protein treated by electron beam irradiation
    • Jin, Y., Liang, R., Liu, J., Lin, S., Yu, Y., Cheng, S., Effect of structure changes on hydrolysis degree, moisture state, and thermal denaturation of egg white protein treated by electron beam irradiation. LWT-Food Science and Technology 77 (2017), 134–141.
    • (2017) LWT-Food Science and Technology , vol.77 , pp. 134-141
    • Jin, Y.1    Liang, R.2    Liu, J.3    Lin, S.4    Yu, Y.5    Cheng, S.6
  • 14
    • 33847028271 scopus 로고    scopus 로고
    • Separation of iron-binding protein from whey through enzymatic hydrolysis
    • Kim, S.B., Seo, I.S., Khan, M.A., Ki, K.S., Nam, M.S., Kim, H.S., Separation of iron-binding protein from whey through enzymatic hydrolysis. International Dairy Journal 17:6 (2007), 625–631.
    • (2007) International Dairy Journal , vol.17 , Issue.6 , pp. 625-631
    • Kim, S.B.1    Seo, I.S.2    Khan, M.A.3    Ki, K.S.4    Nam, M.S.5    Kim, H.S.6
  • 15
    • 58249140350 scopus 로고    scopus 로고
    • Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein
    • Lee, S.H., Song, K.B., Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein. Process Biochemistry 44:3 (2009), 378–381.
    • (2009) Process Biochemistry , vol.44 , Issue.3 , pp. 378-381
    • Lee, S.H.1    Song, K.B.2
  • 16
    • 84988000594 scopus 로고    scopus 로고
    • Antioxidant activity improvement of identified pine nut peptides by pulsed electric field (PEF) and the mechanism exploration
    • Lin, S., Liang, R., Xue, P., Zhang, S., Liu, Z., Dong, X., Antioxidant activity improvement of identified pine nut peptides by pulsed electric field (PEF) and the mechanism exploration. LWT-Food Science and Technology 75 (2017), 366–372.
    • (2017) LWT-Food Science and Technology , vol.75 , pp. 366-372
    • Lin, S.1    Liang, R.2    Xue, P.3    Zhang, S.4    Liu, Z.5    Dong, X.6
  • 17
    • 0027996853 scopus 로고
    • Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy
    • Mach, H., Middaugh, C.R., Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy. Analytical Biochemistry 222:2 (1994), 323–331.
    • (1994) Analytical Biochemistry , vol.222 , Issue.2 , pp. 323-331
    • Mach, H.1    Middaugh, C.R.2
  • 19
    • 65449184945 scopus 로고    scopus 로고
    • Worldwide prevalence of anaemia, WHO vitamin and mineral nutrition information system, 1993–2005
    • McLean, E., Cogswell, M., Egli, I., Wojdyla, D., De Benoist, B., Worldwide prevalence of anaemia, WHO vitamin and mineral nutrition information system, 1993–2005. Public Health Nutrition 12:04 (2009), 444–454.
    • (2009) Public Health Nutrition , vol.12 , Issue.4 , pp. 444-454
    • McLean, E.1    Cogswell, M.2    Egli, I.3    Wojdyla, D.4    De Benoist, B.5
  • 20
    • 77958094134 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of poultry meal with endo-and exopeptidases
    • Nchienzia, H.A., Morawicki, R.O., Gadang, V.P., Enzymatic hydrolysis of poultry meal with endo-and exopeptidases. Poultry Science 89:10 (2010), 2273–2280.
    • (2010) Poultry Science , vol.89 , Issue.10 , pp. 2273-2280
    • Nchienzia, H.A.1    Morawicki, R.O.2    Gadang, V.P.3
  • 21
    • 0031038477 scopus 로고    scopus 로고
    • Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253→ methionine mutant
    • Nicholson, H., Anderson, B.F., Bland, T., Shewry, S.C., Tweedie, J.W., Baker, E.N., Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253→ methionine mutant. Biochemistry 36:2 (1997), 341–346.
    • (1997) Biochemistry , vol.36 , Issue.2 , pp. 341-346
    • Nicholson, H.1    Anderson, B.F.2    Bland, T.3    Shewry, S.C.4    Tweedie, J.W.5    Baker, E.N.6
  • 22
    • 84924956062 scopus 로고    scopus 로고
    • Molecular characterization of whey protein hydrolysate fractions with ferrous chelating and enhanced iron solubility capabilities
    • O'Loughlin, I.B., Kelly, P.M., Murray, B.A., FitzGerald, R.J., Brodkorb, A., Molecular characterization of whey protein hydrolysate fractions with ferrous chelating and enhanced iron solubility capabilities. Journal of Agricultural and Food Chemistry 63:10 (2015), 2708–2714.
    • (2015) Journal of Agricultural and Food Chemistry , vol.63 , Issue.10 , pp. 2708-2714
    • O'Loughlin, I.B.1    Kelly, P.M.2    Murray, B.A.3    FitzGerald, R.J.4    Brodkorb, A.5
  • 23
    • 84875105012 scopus 로고    scopus 로고
    • Meat nutritional composition and nutritive role in the human diet
    • Pereira, P.M.D.C.C., Vicente, A.F.D.R.B., Meat nutritional composition and nutritive role in the human diet. Meat Science 93:3 (2013), 586–592.
    • (2013) Meat Science , vol.93 , Issue.3 , pp. 586-592
    • Pereira, P.M.D.C.C.1    Vicente, A.F.D.R.B.2
  • 24
    • 11844257593 scopus 로고    scopus 로고
    • Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation
    • Puig, S., Askeland, E., Thiele, D.J., Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation. Cell 120:1 (2005), 99–110.
    • (2005) Cell , vol.120 , Issue.1 , pp. 99-110
    • Puig, S.1    Askeland, E.2    Thiele, D.J.3
  • 25
    • 0034284186 scopus 로고    scopus 로고
    • Binding of iron by chicken muscle protein digests: the size of the iron-binding peptides
    • Seth, A., Mahoney, R.R., Binding of iron by chicken muscle protein digests: the size of the iron-binding peptides. Journal of the Science of Food and Agriculture 80:11 (2000), 1595–1600.
    • (2000) Journal of the Science of Food and Agriculture , vol.80 , Issue.11 , pp. 1595-1600
    • Seth, A.1    Mahoney, R.R.2
  • 26
    • 0032172724 scopus 로고    scopus 로고
    • Relationship between some characteristics of WPC hydrolysates and the enzyme complement in commercially available proteinase preparations
    • Smyth, M., FitzGerald, R.J., Relationship between some characteristics of WPC hydrolysates and the enzyme complement in commercially available proteinase preparations. International Dairy Journal 8:9 (1998), 819–827.
    • (1998) International Dairy Journal , vol.8 , Issue.9 , pp. 819-827
    • Smyth, M.1    FitzGerald, R.J.2
  • 27
    • 84885219584 scopus 로고    scopus 로고
    • Global, regional, and national trends in hemoglobin concentration and prevalence of total and severe anaemia in children and pregnant and non-pregnant women for 1995–2011: a systematic analysis of population-representative data
    • Stevens, G.A., Finucane, M.M., De-Regil, L.M., Paciorek, C.J., Flaxman, S.R., Branca, F., Global, regional, and national trends in hemoglobin concentration and prevalence of total and severe anaemia in children and pregnant and non-pregnant women for 1995–2011: a systematic analysis of population-representative data. The Lancet Global Health, 1(1), 2013, 1625.
    • (2013) The Lancet Global Health , vol.1 , Issue.1 , pp. 1625
    • Stevens, G.A.1    Finucane, M.M.2    De-Regil, L.M.3    Paciorek, C.J.4    Flaxman, S.R.5    Branca, F.6
  • 28
    • 33847007267 scopus 로고    scopus 로고
    • Iron-binding properties, amino acid composition, and structure of muscle tissue peptides from in vitro digestion of different meat sources
    • Storcksdieck, S., Bonsmann, G., Hurrell, R.F., 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 (2007), S019–S029.
    • (2007) Journal of Food Science , vol.72 , Issue.1 , pp. S019-S029
    • Storcksdieck, S.1    Bonsmann, G.2    Hurrell, R.F.3
  • 29
    • 84974325042 scopus 로고
    • Application of the plastein reaction to caseins and to skim-milk powder: II. Chemical and physical properties of the plasteins and the mechanism of plastein formation
    • Sukan, G., Andrews, A.T., Application of the plastein reaction to caseins and to skim-milk powder: II. Chemical and physical properties of the plasteins and the mechanism of plastein formation. Journal of Dairy Research 49:02 (1982), 279–293.
    • (1982) Journal of Dairy Research , vol.49 , Issue.2 , pp. 279-293
    • Sukan, G.1    Andrews, A.T.2
  • 31
    • 84861093429 scopus 로고    scopus 로고
    • Iron-chelating activity of chickpea protein hydrolysate peptides
    • Torres-Fuentes, C., Alaiz, M., Vioque, J., Iron-chelating activity of chickpea protein hydrolysate peptides. Food Chemistry 134:3 (2012), 1585–1588.
    • (2012) Food Chemistry , vol.134 , Issue.3 , pp. 1585-1588
    • Torres-Fuentes, C.1    Alaiz, M.2    Vioque, J.3
  • 33
    • 0033832524 scopus 로고    scopus 로고
    • Characterization of food colloids by phase analysis light scattering
    • Vanapalli, S., Coupland, J.N., Characterization of food colloids by phase analysis light scattering. Food Hydrocolloids 14 (2000), 315–317.
    • (2000) Food Hydrocolloids , vol.14 , pp. 315-317
    • Vanapalli, S.1    Coupland, J.N.2
  • 35
    • 28444440308 scopus 로고    scopus 로고
    • Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability
    • Wang, L.L., Xiong, Y.L., Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability. Journal of Agricultural and Food Chemistry 53:23 (2005), 9186–9192.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.23 , pp. 9186-9192
    • Wang, L.L.1    Xiong, Y.L.2
  • 36
    • 79956266692 scopus 로고    scopus 로고
    • Zinc-binding capacity of yak casein hydrolysate and the zinc-releasing characteristics of casein hydrolysate-zinc complexes
    • Wang, X., Zhou, J., Tong, P.S., Mao, X.Y., Zinc-binding capacity of yak casein hydrolysate and the zinc-releasing characteristics of casein hydrolysate-zinc complexes. Journal of Dairy Science 94:6 (2011), 2731–2740.
    • (2011) Journal of Dairy Science , vol.94 , Issue.6 , pp. 2731-2740
    • Wang, X.1    Zhou, J.2    Tong, P.S.3    Mao, X.Y.4
  • 37
    • 84948153454 scopus 로고    scopus 로고
    • Identification of antioxidant peptides from protein hydrolysates of scallop (Patinopecten yessoensis) female gonads
    • Wu, H.T., Jin, W.G., Sun, S.G., Li, X.S., Duan, X.H., Li, Y., Identification of antioxidant peptides from protein hydrolysates of scallop (Patinopecten yessoensis) female gonads. European Food Research and Technology 242:5 (2016), 713–722.
    • (2016) European Food Research and Technology , vol.242 , Issue.5 , pp. 713-722
    • Wu, H.T.1    Jin, W.G.2    Sun, S.G.3    Li, X.S.4    Duan, X.H.5    Li, Y.6
  • 38
    • 84862255065 scopus 로고    scopus 로고
    • Enzymatic preparation and characterization of iron-chelating peptides from anchovy (Engraulis japonicus) muscle protein
    • Wu, H., Liu, Z., Zhao, Y., Zeng, M., Enzymatic preparation and characterization of iron-chelating peptides from anchovy (Engraulis japonicus) muscle protein. Food Research International 48:2 (2012), 435–441.
    • (2012) Food Research International , vol.48 , Issue.2 , pp. 435-441
    • Wu, H.1    Liu, Z.2    Zhao, Y.3    Zeng, M.4
  • 39
    • 84900480112 scopus 로고    scopus 로고
    • Iron binding capacity of dephytinised soy protein isolate hydrolysate as influenced by the degree of hydrolysis and enzyme type
    • Zhang, M.N., Huang, G.R., Jiang, J.X., Iron binding capacity of dephytinised soy protein isolate hydrolysate as influenced by the degree of hydrolysis and enzyme type. Journal of Food Science and Technology 51:5 (2014), 994–999.
    • (2014) Journal of Food Science and Technology , vol.51 , Issue.5 , pp. 994-999
    • Zhang, M.N.1    Huang, G.R.2    Jiang, J.X.3
  • 40
    • 84864060915 scopus 로고    scopus 로고
    • Preparation and characterization of β-lactoglobulin hydrolysate-iron complexes
    • Zhou, J., Wang, X., Ai, T., Cheng, X., Guo, H.Y., Teng, G.X., Mao, X.Y., Preparation and characterization of β-lactoglobulin hydrolysate-iron complexes. Journal of Dairy Science 95:8 (2012), 4230–4236.
    • (2012) Journal of Dairy Science , vol.95 , Issue.8 , pp. 4230-4236
    • Zhou, J.1    Wang, X.2    Ai, T.3    Cheng, X.4    Guo, H.Y.5    Teng, G.X.6    Mao, X.Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.