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Volumn 17, Issue 5, 2004, Pages 712-718

Separation of calcium-binding protein derived from enzymatic hydrolysates of cheese whey protein

Author keywords

Calcium binding Protein; Cheese Whey Protein; Enzymatic Hydrolysates

Indexed keywords


EID: 4344590553     PISSN: 10112367     EISSN: None     Source Type: Journal    
DOI: 10.5713/ajas.2004.712     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0030586806 scopus 로고    scopus 로고
    • Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity
    • Adamson, N. J. and E. C. Reynolds. 1996. Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity. Enzyme Microb. Tech. 19:202.
    • (1996) Enzyme Microb. Tech. , vol.19 , pp. 202
    • Adamson, N.J.1    Reynolds, E.C.2
  • 3
    • 4344714670 scopus 로고    scopus 로고
    • Dairy components increasingly find uses in functional foods
    • April
    • Anon. 1998. Dairy components increasingly find uses in functional foods. The cheese reporter, April. 10:11.
    • (1998) The Cheese Reporter , vol.10 , pp. 11
  • 4
    • 0041885362 scopus 로고    scopus 로고
    • Thermal modifications of structure and co-denaturation of α-lactalbumin and β-lactoglobulin induce changes of solubility and susceptibility to proteases
    • Bertrand-Harb, C., A. Baday, M. Dalgalarrondo, J. M. Chobert and T. Haetle. 2002. Thermal modifications of structure and co-denaturation of α-lactalbumin and β-lactoglobulin induce changes of solubility and susceptibility to proteases. Nahrung. 46:283.
    • (2002) Nahrung. , vol.46 , pp. 283
    • Bertrand-Harb, C.1    Baday, A.2    Dalgalarrondo, M.3    Chobert, J.M.4    Haetle, T.5
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive methods for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive methods for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 6
    • 0002655843 scopus 로고
    • The role of calcium in a balanced diet
    • Buttriss, J. 1990. The role of calcium in a balanced diet. J. Soc. Dairy Tech. 48:1.
    • (1990) J. Soc. Dairy Tech. , vol.48 , pp. 1
    • Buttriss, J.1
  • 7
    • 33845280838 scopus 로고
    • Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin
    • Chobert, J. M., C. Bertrand-Harb and M. G. Nicolas. 1988. Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J. Agr. Food Chem. 36:883.
    • (1988) J. Agr. Food Chem. , vol.36 , pp. 883
    • Chobert, J.M.1    Bertrand-Harb, C.2    Nicolas, M.G.3
  • 8
    • 0036224503 scopus 로고    scopus 로고
    • Process-induced changes in whey proteins during the manufacture of whey protein concentrates
    • De la Fuente, M. A., Y. Hemar, M. Tamehara, P. A. Munro and H. Singh. 2002. Process-induced changes in whey proteins during the manufacture of whey protein concentrates. Int. Dairy J. 12:361.
    • (2002) Int. Dairy J. , vol.12 , pp. 361
    • De La Fuente, M.A.1    Hemar, Y.2    Tamehara, M.3    Munro, P.A.4    Singh, H.5
  • 9
    • 0010365792 scopus 로고
    • Food preference and the opioid peptide system
    • Drewnowski, A. 1992. Food preference and the opioid peptide system. Trends Food Sci. Tech. 3:97.
    • (1992) Trends Food Sci. Tech. , vol.3 , pp. 97
    • Drewnowski, A.1
  • 10
    • 0040937831 scopus 로고    scopus 로고
    • Lactokinins: Whey protein-derived ACE inhibitory peptides
    • FitzGerald, R. J. and H. Meisel. 1999. Lactokinins: whey protein-derived ACE inhibitory peptides. Nahrung. 43:165.
    • (1999) Nahrung. , vol.43 , pp. 165
    • FitzGerald, R.J.1    Meisel, H.2
  • 12
    • 0018848374 scopus 로고
    • Purification of chick intestinal calcium-binding protein
    • Friedlander, E. J. and A. W. Norman. 1980. Purification of chick intestinal calcium-binding protein. Methods in Enzymology 67:504.
    • (1980) Methods in Enzymology , vol.67 , pp. 504
    • Friedlander, E.J.1    Norman, A.W.2
  • 13
    • 85039505800 scopus 로고    scopus 로고
    • Bioactive and nutraceutical entities found in whey
    • Paper presented June Atlanta, Georgia, USA
    • Gallaher, D. and M. Schmidl. 1998. Bioactive and nutraceutical entities found in whey. Paper presented at Institute of Food Technologists, Annual Meeting, June Atlanta, Georgia, USA.
    • (1998) Institute of Food Technologists, Annual Meeting
    • Gallaher, D.1    Schmidl, M.2
  • 14
    • 0029398314 scopus 로고
    • Susceptibility of β-Lactoglobulin and Sodium Caseinate to Proteolysis by Pepsin and Trypsin
    • Guo, M. R., P. F. Fox and A. Flynn. 1995. Susceptibility of β-Lactoglobulin and Sodium Caseinate to Proteolysis by Pepsin and Trypsin. J. Dairy Sci. 78:2336.
    • (1995) J. Dairy Sci. , vol.78 , pp. 2336
    • Guo, M.R.1    Fox, P.F.2    Flynn, A.3
  • 16
    • 0017528647 scopus 로고
    • Partial enzymatic hydrolysis of whey protein by trypsin
    • Jost, R. and J. C. Monti. 1977. Partial enzymatic hydrolysis of whey protein by trypsin. J. Dairy Sci. 60:1387.
    • (1977) J. Dairy Sci. , vol.60 , pp. 1387
    • Jost, R.1    Monti, J.C.2
  • 17
    • 0000084237 scopus 로고
    • Enzyme-modified protein food ingredients
    • Kilara, A. 1985. Enzyme-modified protein food ingredients. Biochem. 20:149.
    • (1985) Biochem. , vol.20 , pp. 149
    • Kilara, A.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lord). 227:680.
    • (1970) Nature (Lord) , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 23
    • 0030375693 scopus 로고    scopus 로고
    • Bioactive peptides derived from milk proteins: Ingredients for functional food?
    • Meisel, H. and E. Schlimme. 1996. Bioactive peptides derived from milk proteins: ingredients for functional food? Kieler Milchwissenschaftliche Forshungsbeirchte. 48:343.
    • (1996) Kieler Milchwissenschaftliche Forshungsbeirchte , vol.48 , pp. 343
    • Meisel, H.1    Schlimme, E.2
  • 24
    • 0024794090 scopus 로고
    • Calcium in the diet, food sources, recommanded intakes and nutritional bioavailability
    • Miller, D. D. 1989. Calcium in the diet, food sources, recommanded intakes and nutritional bioavailability. Adv. Food Nutr. Res. 33:103.
    • (1989) Adv. Food Nutr. Res. , vol.33 , pp. 103
    • Miller, D.D.1
  • 25
    • 84986502507 scopus 로고
    • Enzymatic solubilization of heat-denatured cheese whey protein
    • Monti, J. C. and R. Jost. 1978. Enzymatic solubilization of heat-denatured cheese whey protein. J. Dairy Sci. 61:1233.
    • (1978) J. Dairy Sci. , vol.61 , pp. 1233
    • Monti, J.C.1    Jost, R.2
  • 26
    • 0031464182 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digestes of whey protein
    • Mullally, M. M., H. Meisel and R. J. FitzGerald. 1997. Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digestes of whey protein. Int. Dairy J. 7:299.
    • (1997) Int. Dairy J. , vol.7 , pp. 299
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 27
    • 0036134708 scopus 로고    scopus 로고
    • Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin
    • Noyelle, K. and H. van Deal. 2002. Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin. J. Inorganic Biochem. 88:69.
    • (2002) J. Inorganic Biochem. , vol.88 , pp. 69
    • Noyelle, K.1    Van Deal, H.2
  • 28
    • 0031582834 scopus 로고    scopus 로고
    • Hydrolysis of bovine β-lactoglobulin by various protease and identification of selected peptides
    • Otte, J., M. Zakora, K. B. Qvist, C. E. Olsen and V. Barkholt. 1997. Hydrolysis of bovine β-lactoglobulin by various protease and identification of selected peptides. Int. Dairy J. 7:835.
    • (1997) Int. Dairy J. , vol.7 , pp. 835
    • Otte, J.1    Zakora, M.2    Qvist, K.B.3    Olsen, C.E.4    Barkholt, V.5
  • 30
    • 0027323385 scopus 로고
    • Allergenicity of milk protein hydrolysate formulae in children with cow milk allergy
    • Ragno, V., P. G. Giampietro, G. Bruno and L. Businco. 1993. Allergenicity of milk protein hydrolysate formulae in children with cow milk allergy. Eur. J. Pediatr. 152:760.
    • (1993) Eur. J. Pediatr. , vol.152 , pp. 760
    • Ragno, V.1    Giampietro, P.G.2    Bruno, G.3    Businco, L.4
  • 31
    • 0028706866 scopus 로고
    • Dairy foods: Dairy calcium, bone metabolism and prevention of osteoporosis
    • Renner, E. 1994. Dairy foods: dairy calcium, bone metabolism and prevention of osteoporosis. J. Dairy Sci. 77:3498.
    • (1994) J. Dairy Sci. , vol.77 , pp. 3498
    • Renner, E.1
  • 33
    • 85010245780 scopus 로고
    • Quantitative determination of the major components of casein mixture by column chromatography on DEAE-cellulose
    • Rose, D., D. T. Davies and M. Yaguchi. 1969. Quantitative determination of the major components of casein mixture by column chromatography on DEAE-cellulose. J. Dairy Sci. 52:8.
    • (1969) J. Dairy Sci. , vol.52 , pp. 8
    • Rose, D.1    Davies, D.T.2    Yaguchi, M.3
  • 34
    • 0001769758 scopus 로고
    • Enzymatic hydrolysis of whey proteins. Influence of heat treatment of α-LA and β-LG on their proteolysis by pepsin and papain
    • Schmidt, D. G. and B. W. van Markwijk. 1993. Enzymatic hydrolysis of whey proteins. Influence of heat treatment of α-LA and β-LG on their proteolysis by pepsin and papain. Neth. Milk Dairy J. 47:15.
    • (1993) Neth. Milk Dairy J. , vol.47 , pp. 15
    • Schmidt, D.G.1    Van Markwijk, B.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.