메뉴 건너뛰기




Volumn 5, Issue 2, 2013, Pages 689-697

Purification and characterisation of a zinc-binding peptide from oyster protein hydrolysate

Author keywords

Hydrolysates; Immobilised metal affinity chromatography; Oyster protein; Zinc binding peptide

Indexed keywords

OSTREIDAE;

EID: 84876731664     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2013.01.012     Document Type: Article
Times cited : (134)

References (40)
  • 1
    • 84890571156 scopus 로고    scopus 로고
    • Zinc and immune function: The biological basis of altered resistance to infection
    • Anuraj H.S., Ananda S.P. Zinc and immune function: The biological basis of altered resistance to infection. The American Journal of Clinical Nutrition 1998, 68:63S-447S.
    • (1998) The American Journal of Clinical Nutrition , vol.68
    • Anuraj, H.S.1    Ananda, S.P.2
  • 4
    • 85008212530 scopus 로고
    • Laboratory evaluations of solubility and structural integrity of complexed and chelated trace mineral supplements
    • Brown T.F., Zeringue L.K. Laboratory evaluations of solubility and structural integrity of complexed and chelated trace mineral supplements. Journal of Dairy Science 1994, 77:181-189.
    • (1994) Journal of Dairy Science , vol.77 , pp. 181-189
    • Brown, T.F.1    Zeringue, L.K.2
  • 6
    • 0039693128 scopus 로고    scopus 로고
    • Characterization of organic zinc sources and their relative bioavailabilities for poultry and sheep
    • Ph.D. thesis, America: University of Florida.
    • Cao, J. (1998). Characterization of organic zinc sources and their relative bioavailabilities for poultry and sheep (pp. 23-125). Ph.D. thesis, America: University of Florida.
    • (1998) , pp. 23-125
    • Cao, J.1
  • 7
    • 0002384554 scopus 로고    scopus 로고
    • Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein
    • Chen H.M., Muramoto K., Yamauch I.F., Fujimoto K., Nokihara K. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. Journal of Agriculture and Food Chemistry 1998, 46:49-53.
    • (1998) Journal of Agriculture and Food Chemistry , vol.46 , pp. 49-53
    • Chen, H.M.1    Muramoto, K.2    Yamauch, I.F.3    Fujimoto, K.4    Nokihara, K.5
  • 9
    • 68149156928 scopus 로고    scopus 로고
    • Peptide length, steric effects, and ion solvation govern zwitterion stabilization in barium-chelated di- and tripeptides
    • Dunbar R.C., Steill J.D., Polfer N.C., Oomens J. Peptide length, steric effects, and ion solvation govern zwitterion stabilization in barium-chelated di- and tripeptides. The Journal of Physical Chemistry B 2009, 113:10552-10554.
    • (2009) The Journal of Physical Chemistry B , vol.113 , pp. 10552-10554
    • Dunbar, R.C.1    Steill, J.D.2    Polfer, N.C.3    Oomens, J.4
  • 10
    • 0027323183 scopus 로고
    • Secondary structure and temperature-induced unfolding and refolding of ribonuclease-T1 in aqueous solution - a Fourier transform infrared spectroscopy study
    • Fabian H.C., Schultz D., Naumann D., Landt O., Hahn U., Saenger W. Secondary structure and temperature-induced unfolding and refolding of ribonuclease-T1 in aqueous solution - a Fourier transform infrared spectroscopy study. Journal of Molecular Biology 1993, 232:967-981.
    • (1993) Journal of Molecular Biology , vol.232 , pp. 967-981
    • Fabian, H.C.1    Schultz, D.2    Naumann, D.3    Landt, O.4    Hahn, U.5    Saenger, W.6
  • 11
    • 84871810337 scopus 로고    scopus 로고
    • FAO, Rome, Food and Agriculture Organization (FAO)
    • Food and Agriculture Organization (FAO) FAO yearbook, fishery and aquaculture statistics 2012, FAO, Rome, pp. 50-51.
    • (2012) FAO yearbook, fishery and aquaculture statistics , pp. 50-51
  • 12
    • 77955042227 scopus 로고    scopus 로고
    • Influence of feeding diets supplements with different levels and sources of zinc, copper and manganese on the mineral concentrations in tibia and performance of broiler chickens
    • Gheisari A.A., Fathkoohi A.R., Toghyani M., Gheisari M.M. Influence of feeding diets supplements with different levels and sources of zinc, copper and manganese on the mineral concentrations in tibia and performance of broiler chickens. Asian Journal of Animal and Veterinary Advance 2011, 6:166-174.
    • (2011) Asian Journal of Animal and Veterinary Advance , vol.6 , pp. 166-174
    • Gheisari, A.A.1    Fathkoohi, A.R.2    Toghyani, M.3    Gheisari, M.M.4
  • 14
  • 15
    • 84857689220 scopus 로고    scopus 로고
    • Bioactive peptides from marine processing waste and shellfish: A review
    • Harnedy P.A., FitzGerald R.J. Bioactive peptides from marine processing waste and shellfish: A review. Journal of Functional Foods 2012, 4:6-24.
    • (2012) Journal of Functional Foods , vol.4 , pp. 6-24
    • Harnedy, P.A.1    FitzGerald, R.J.2
  • 16
    • 77957920876 scopus 로고    scopus 로고
    • Metals in protein structures: A review of their principal features
    • Harding M.M., Nowichi M.W., Walkinshaw M.D. Metals in protein structures: A review of their principal features. Crystallography Reviews 2010, 16:247-302.
    • (2010) Crystallography Reviews , vol.16 , pp. 247-302
    • Harding, M.M.1    Nowichi, M.W.2    Walkinshaw, M.D.3
  • 18
    • 33847757801 scopus 로고    scopus 로고
    • Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame
    • Jung W.K., Kim S.K. Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame. European Food Research and Technology 2007, 224:763-767.
    • (2007) European Food Research and Technology , vol.224 , pp. 763-767
    • Jung, W.K.1    Kim, S.K.2
  • 19
    • 20444397021 scopus 로고    scopus 로고
    • Copper (II) complexes of oligopeptides containing aspartyl and glutamyl residues. Potentiometric and spectroscopic studies
    • Kallay C., Varnagy K., Micera G., Sanna D., Sovago I. Copper (II) complexes of oligopeptides containing aspartyl and glutamyl residues. Potentiometric and spectroscopic studies. Journal of Inorganic Biochemistry 2005, 99:1514-1525.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , pp. 1514-1525
    • Kallay, C.1    Varnagy, K.2    Micera, G.3    Sanna, D.4    Sovago, I.5
  • 20
    • 77349090649 scopus 로고    scopus 로고
    • Development and biological activities of marine-derived bioactive peptides: A review
    • Kim S.K., Wijesekara I. Development and biological activities of marine-derived bioactive peptides: A review. Journal of Functional Foods 2010, 2:1-9.
    • (2010) Journal of Functional Foods , vol.2 , pp. 1-9
    • Kim, S.K.1    Wijesekara, I.2
  • 21
    • 34447599642 scopus 로고
    • Neue methode zur bestimmung des stickstoffs in organischen korpern
    • Kjeldahl J. Neue methode zur bestimmung des stickstoffs in organischen korpern. Analytical and Bioanalytical Chemistry 1883, 22:366-382.
    • (1883) Analytical and Bioanalytical Chemistry , vol.22 , pp. 366-382
    • Kjeldahl, J.1
  • 22
    • 64549156088 scopus 로고    scopus 로고
    • Milk-derived bioactive peptides: From science to applications
    • Korhonen H. Milk-derived bioactive peptides: From science to applications. Journal of Functional Foods 2009, 1:177-187.
    • (2009) Journal of Functional Foods , vol.1 , pp. 177-187
    • Korhonen, H.1
  • 24
    • 58249140350 scopus 로고    scopus 로고
    • Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein
    • Lee L.H., Song K.B. Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein. Process Biochemistry 2009, 44:378-381.
    • (2009) Process Biochemistry , vol.44 , pp. 378-381
    • Lee, L.H.1    Song, K.B.2
  • 27
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • Nielsen P.M., Petersen D., Dambamann C. Improved method for determining food protein degree of hydrolysis. Journal of Food Science 2001, 66:642-646.
    • (2001) Journal of Food Science , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambamann, C.3
  • 28
    • 0032463144 scopus 로고    scopus 로고
    • Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of β-casein
    • Peres J.M., Bouhallab S., Petit C., Bureau F., Maubois J.L., Arhan P., Bougle D. Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of β-casein. Reproduction Nutrition Development 1998, 12:465-472.
    • (1998) Reproduction Nutrition Development , vol.12 , pp. 465-472
    • Peres, J.M.1    Bouhallab, S.2    Petit, C.3    Bureau, F.4    Maubois, J.L.5    Arhan, P.6    Bougle, D.7
  • 29
    • 0021114727 scopus 로고
    • Immobilized metal affinity adsorption and immobilized metal affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions
    • Porath J., Olin B. Immobilized metal affinity adsorption and immobilized metal affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions. Biochemistry 1983, 22:1621-1630.
    • (1983) Biochemistry , vol.22 , pp. 1621-1630
    • Porath, J.1    Olin, B.2
  • 30
    • 84860271848 scopus 로고    scopus 로고
    • Advance on small peptide promoting absorption of trace mineral
    • (in Chinese)
    • Qiao W., Zhou A.G., Wang Z.S., Bin S.Y. Advance on small peptide promoting absorption of trace mineral. Feed Industry 2006, 27:12-14. (in Chinese).
    • (2006) Feed Industry , vol.27 , pp. 12-14
    • Qiao, W.1    Zhou, A.G.2    Wang, Z.S.3    Bin, S.Y.4
  • 31
    • 20444439584 scopus 로고    scopus 로고
    • Synthesis and characterization of mixed ligand complex of Zn (II) and Co (II) with amino acids: Relevance to zinc binding sites in zinc fingers
    • Reddy P., Radhika M., Manjula P. Synthesis and characterization of mixed ligand complex of Zn (II) and Co (II) with amino acids: Relevance to zinc binding sites in zinc fingers. Journal of Chemical Sciences 2005, 117:239-246.
    • (2005) Journal of Chemical Sciences , vol.117 , pp. 239-246
    • Reddy, P.1    Radhika, M.2    Manjula, P.3
  • 33
    • 0020561378 scopus 로고
    • Ligands of binding cadmium, zinc, and copper in a species of New Zealand oyster (Ostrea lutaria)
    • Sharama R.P. Ligands of binding cadmium, zinc, and copper in a species of New Zealand oyster (Ostrea lutaria). Bulletin of Environmental Contamination and Toxicology 1983, 30:428-434.
    • (1983) Bulletin of Environmental Contamination and Toxicology , vol.30 , pp. 428-434
    • Sharama, R.P.1
  • 34
    • 0343320717 scopus 로고
    • Coordinating properties of the amide bond. Stability and structure of metal ion complexes of peptides and related ligands
    • Sigel H., Martin R.B. Coordinating properties of the amide bond. Stability and structure of metal ion complexes of peptides and related ligands. Chemical Reviews 1982, 82:385-426.
    • (1982) Chemical Reviews , vol.82 , pp. 385-426
    • Sigel, H.1    Martin, R.B.2
  • 36
    • 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 2007, 72:S19-S29.
    • (2007) Journal of Food Science , vol.72
    • Storcksdieck, S.1    Bonsmann, G.2    Hurrell, R.F.3
  • 39
    • 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 2011, 94:2731-2740.
    • (2011) Journal of Dairy Science , vol.94 , pp. 2731-2740
    • Wang, X.1    Zhou, J.2    Tong, P.S.3    Mao, X.Y.4
  • 40
    • 0030447656 scopus 로고    scopus 로고
    • Metal binding properties and secondary structure of the zinc-binding domain of Nup475
    • Worthington M.T., Amann B.T., Nathans D., Berg J.M. Metal binding properties and secondary structure of the zinc-binding domain of Nup475. Biochemistry 1996, 93:13754-13759.
    • (1996) Biochemistry , vol.93 , pp. 13754-13759
    • Worthington, M.T.1    Amann, B.T.2    Nathans, D.3    Berg, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.