메뉴 건너뛰기




Volumn 236, Issue 1, 2013, Pages 57-63

Calcium-binding peptides derived from tilapia (Oreochromis niloticus) protein hydrolysate

Author keywords

Alcalase 2.4 L; Calcium binding peptide; Oreochromis niloticus; Protein hydrolysate; Tilapia protein

Indexed keywords

ALCALASE; CALCIUM BINDING; DEGREE OF HYDROLYSIS; EDMAN DEGRADATION; GEL-FILTRATION CHROMATOGRAPHY; OREOCHROMIS NILOTICUS; PROTEIN HYDROLYSATE; SEPHADEX;

EID: 84871927344     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-012-1860-2     Document Type: Article
Times cited : (100)

References (34)
  • 1
    • 84871920204 scopus 로고    scopus 로고
    • Department of Fisheries Thailand, (Online). Available (1 September 2011)
    • Department of Fisheries Thailand (2011) Strategic development of tilapia (2010-2014) (Online). Available http://www. fisheries. go. th/dof/ (1 September 2011).
    • (2011) Strategic development of tilapia (2010-2014)
  • 2
    • 78149286952 scopus 로고    scopus 로고
    • Chemical and physicochemical properties of tilapia (Oreochromis niloticus) fish protein hydrolysate and concentrate
    • 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 Bio Chem 5: 21-36.
    • (2011) Int J Bio Chem , vol.5 , pp. 21-36
    • Foh, M.B.K.1    Kamara, M.T.2    Amadou, I.3    Foh, B.M.4    Wenshui, X.5
  • 3
    • 77951899969 scopus 로고    scopus 로고
    • and antioxidant properties of tilapia (Oreochromis niloticus) as influenced by Functionality the degree of hydrolysis
    • Foh MBK, Amadou I, Foh BM, Kamara MT, Xia W (2010) and antioxidant properties of tilapia (Oreochromis niloticus) as influenced by Functionality the degree of hydrolysis. Int J Mol Sci 11: 1851-1869.
    • (2010) Int J Mol Sci , vol.11 , pp. 1851-1869
    • Foh, M.B.K.1    Amadou, I.2    Foh, B.M.3    Kamara, M.T.4    Xia, W.5
  • 4
    • 67649321434 scopus 로고    scopus 로고
    • ACE-inhibitory activity of tilapia protein hydrolysates
    • Raghavan S, Kristinsson HG (2009) ACE-inhibitory activity of tilapia protein hydrolysates. Food Chem 117: 582-588.
    • (2009) Food Chem , vol.117 , pp. 582-588
    • Raghavan, S.1    Kristinsson, H.G.2
  • 8
    • 0023449673 scopus 로고
    • Calcium in dairy products
    • Tunick MH (1987) Calcium in dairy products. J Dairy Sci 70: 2429-2438.
    • (1987) J Dairy Sci , vol.70 , pp. 2429-2438
    • Tunick, M.H.1
  • 9
    • 0032930793 scopus 로고    scopus 로고
    • Nutrition Aspects of Calcium Absorption
    • Bronner F, Pansu D (1998) Nutrition Aspects of Calcium Absorption. J Nutr 129: 9-12.
    • (1998) J Nutr , vol.129 , pp. 9-12
    • Bronner, F.1    Pansu, D.2
  • 10
    • 13444254466 scopus 로고    scopus 로고
    • Description of an individual patient methodology for calculating the cost effectiveness of treatments for osteoporosis in women
    • Stevenson MD, Brazier JE, Calvert NW, Lloyd-Jones M, Oakley J, Kanis JA (2005) Description of an individual patient methodology for calculating the cost effectiveness of treatments for osteoporosis in women. J Oper Res Soc 56: 214-221.
    • (2005) J Oper Res Soc , vol.56 , pp. 214-221
    • Stevenson, M.D.1    Brazier, J.E.2    Calvert, N.W.3    Lloyd-Jones, M.4    Oakley, J.5    Kanis, J.A.6
  • 11
    • 78049407512 scopus 로고    scopus 로고
    • Isolation of a calcium-binding peptide from enzymatic hydrolyzates of porcine blood plasma protein
    • Lee SH, Song KB (2009) Isolation of a calcium-binding peptide from enzymatic hydrolyzates of porcine blood plasma protein. J Appl biol chem (Korean Soc Appl Biol Chem) 52: 290-294.
    • (2009) J Appl Biol Chem (Korean Soc Appl Biol Chem) , vol.52 , pp. 290-294
    • Lee, S.H.1    Song, K.B.2
  • 12
    • 0015919789 scopus 로고
    • Carp muscle calcium-binding protein I. characterization of the tryptic peptides and the complete amino acid sequence of component B
    • Coffee CJ, Bradshaw RA (1973) Carp muscle calcium-binding protein I. characterization of the tryptic peptides and the complete amino acid sequence of component B. J Biol Chem 248: 3305-3312.
    • (1973) J Biol Chem , vol.248 , pp. 3305-3312
    • Coffee, C.J.1    Bradshaw, R.A.2
  • 13
    • 33746380547 scopus 로고    scopus 로고
    • Recovery of a novel Ca-binding peptide from Alaska Pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis
    • Jung WK, Karawita R, Heo SJ, Lee BJ, Kim SK, Jeon YJ (2006) Recovery of a novel Ca-binding peptide from Alaska Pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis. Process Biochem 41: 2097-2100.
    • (2006) Process Biochem , vol.41 , pp. 2097-2100
    • Jung, W.K.1    Karawita, R.2    Heo, S.J.3    Lee, B.J.4    Kim, S.K.5    Jeon, Y.J.6
  • 14
    • 33847757801 scopus 로고    scopus 로고
    • Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame
    • Jung WK, Kim SK (2007) Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame. Eur Food Res Tech 224: 763-767.
    • (2007) Eur Food Res Tech , vol.224 , pp. 763-767
    • Jung, W.K.1    Kim, S.K.2
  • 15
    • 34548292478 scopus 로고    scopus 로고
    • Calcium-binding ability of soy protein hydrolysates
    • Bao XL, Song M, Zhang J, Chen Y, Guo ST (2007) Calcium-binding ability of soy protein hydrolysates. Chin Chem Lett 18: 1115-1118.
    • (2007) Chin Chem Lett , vol.18 , pp. 1115-1118
    • Bao, X.L.1    Song, M.2    Zhang, J.3    Chen, Y.4    Guo, S.T.5
  • 16
    • 78751648551 scopus 로고    scopus 로고
    • Purification of a histidine-containing peptide with calcium binding activity from shrimp processing byproducts hydrolysate
    • Huang G, Ren L, Jiang J (2011) Purification of a histidine-containing peptide with calcium binding activity from shrimp processing byproducts hydrolysate. Eur Food Res Tech 232: 281-287.
    • (2011) Eur Food Res Tech , vol.232 , pp. 281-287
    • Huang, G.1    Ren, L.2    Jiang, J.3
  • 19
    • 40549121909 scopus 로고    scopus 로고
    • Antioxidative efficacy of alkali-treated tilapia protein hydrolysates: a comparative study of five enzymes
    • Raghavan S, Kristinsson HG (2008) Antioxidative efficacy of alkali-treated tilapia protein hydrolysates: a comparative study of five enzymes. J Agric Food Chem 56: 1434-1441.
    • (2008) J Agric Food Chem , vol.56 , pp. 1434-1441
    • Raghavan, S.1    Kristinsson, H.G.2
  • 20
    • 77955590616 scopus 로고    scopus 로고
    • AOAC, 16th ed. Association of Official Agricultural Chemists, Inc. Washington, D.C
    • AOAC (1999) AOAC official methods of analysis 16th ed. Association of Official Agricultural Chemists, Inc. Washington, D. C.
    • (1999) AOAC official methods of analysis
  • 21
    • 0036221936 scopus 로고    scopus 로고
    • Preparation and characterization of hydrolyzed proteins from defibrinated bovine plasma
    • Wanasundara PKJPD, Amarowicz R, Pegg RB, Shand PJ (2002) Preparation and characterization of hydrolyzed proteins from defibrinated bovine plasma. J Food Sci 67: 623-630.
    • (2002) J Food Sci , vol.67 , pp. 623-630
    • Wanasundara, P.K.J.P.D.1    Amarowicz, R.2    Pegg, R.B.3    Shand, P.J.4
  • 22
    • 0000130569 scopus 로고
    • Multiple range and multiple F tests
    • Duncan DB (1995) Multiple range and multiple F tests. Biometrics 11: 1-42.
    • (1995) Biometrics , vol.11 , pp. 1-42
    • Duncan, D.B.1
  • 23
    • 0001797666 scopus 로고
    • Seafood processing byproducts
    • 1st edn., F. Shahidi and J. R. Botta (Eds.), London: Blackie
    • Shahidi F (1994) Seafood processing byproducts. In: Shahidi F, Botta JR (eds) Seafoods: chemistry, processing technology and quality, 1st edn. Blackie, London, pp 321-324.
    • (1994) Seafoods: Chemistry, Processing Technology and Quality , pp. 321-324
    • Shahidi, F.1
  • 24
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom L (2002) Serine protease mechanism and specificity. Chem Rev 102: 4501-4524.
    • (2002) Chem Rev , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 25
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto HH, Schirmeister T (1997) Cysteine proteases and their inhibitors. Chem Rev 97: 133-171.
    • (1997) Chem Rev , vol.97 , pp. 133-171
    • Otto, H.H.1    Schirmeister, T.2
  • 26
    • 85036174305 scopus 로고    scopus 로고
    • Extracellular leucine aminopeptidase produced by Aspergillus oryzae LL1 and LL2
    • Lin SJ, Chen LL, Wen CY, Chu WS (2010) Extracellular leucine aminopeptidase produced by Aspergillus oryzae LL1 and LL2. Afr J Microbiol Res 4: 158-168.
    • (2010) Afr J Microbiol Res , vol.4 , pp. 158-168
    • Lin, S.J.1    Chen, L.L.2    Wen, C.Y.3    Chu, W.S.4
  • 27
    • 34548654506 scopus 로고    scopus 로고
    • Hydrolysis of rapeseed protein isolates: kinetics, characterization and functional properties of hydrolyzates
    • Chabanon G, Chevalot I, Framboisier X, Chenu S, Narc I (2007) Hydrolysis of rapeseed protein isolates: kinetics, characterization and functional properties of hydrolyzates. Process Biochem 42: 1419-1428.
    • (2007) Process Biochem , vol.42 , pp. 1419-1428
    • Chabanon, G.1    Chevalot, I.2    Framboisier, X.3    Chenu, S.4    Narc, I.5
  • 29
    • 33746916060 scopus 로고    scopus 로고
    • Improvement of gelling properties of porcine blood plasma using microbial transglutaminase
    • Saguer E, Fort N, Parses D, Toldra M, Carretero C (2007) Improvement of gelling properties of porcine blood plasma using microbial transglutaminase. Food Chem 101: 49-56.
    • (2007) Food Chem , vol.101 , pp. 49-56
    • Saguer, E.1    Fort, N.2    Parses, D.3    Toldra, M.4    Carretero, C.5
  • 30
    • 79957646210 scopus 로고    scopus 로고
    • Surface characterization of 7S and 11S globulin powders from soy protein examined by X-ray photoelectron spectroscopy and scanning electron microscopy
    • Zhao X, Chen J, Zhu Q, Du F, Ao Q, Liu J (2011) Surface characterization of 7S and 11S globulin powders from soy protein examined by X-ray photoelectron spectroscopy and scanning electron microscopy. Colloids Surf B Biointerface 86: 260-266.
    • (2011) Colloids Surf B Biointerface , vol.86 , pp. 260-266
    • Zhao, X.1    Chen, J.2    Zhu, Q.3    Du, F.4    Ao, Q.5    Liu, J.6
  • 31
    • 0036597798 scopus 로고    scopus 로고
    • Soy protein: its effects on intestinal calcium transport, serum vitamin D, and insulin-like growth factor-I in ovariectomized rats
    • Arjmandi BH, Khalil DA, Hollis BW (2002) Soy protein: its effects on intestinal calcium transport, serum vitamin D, and insulin-like growth factor-I in ovariectomized rats. Calcif Tissue Int 70: 483-487.
    • (2002) Calcif Tissue Int , vol.70 , pp. 483-487
    • Arjmandi, B.H.1    Khalil, D.A.2    Hollis, B.W.3
  • 33
    • 0032245504 scopus 로고    scopus 로고
    • Determination of calcium binding sites in gas-phase small peptides by tandem mass spectrometry
    • Nemirovskiy OV, Gross ML (1998) Determination of calcium binding sites in gas-phase small peptides by tandem mass spectrometry. J Amer Soc Mass Spectrom 9: 1020-1028.
    • (1998) J Amer Soc Mass Spectrom , vol.9 , pp. 1020-1028
    • Nemirovskiy, O.V.1    Gross, M.L.2
  • 34
    • 0000958755 scopus 로고
    • Effect of pH on the binding of calcium ions by soybean proteins
    • Kroll RD (1984) Effect of pH on the binding of calcium ions by soybean proteins. Cer Chem 61: 490-495.
    • (1984) Cer Chem , vol.61 , pp. 490-495
    • Kroll, R.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.