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Volumn 18, Issue 12, 2008, Pages 1097-1102

Kinetic characterization of hydrolysis of camel and bovine milk proteins by pancreatic enzymes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; FOOD PRODUCTS PLANTS;

EID: 51049089942     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2008.06.003     Document Type: Article
Times cited : (92)

References (31)
  • 1
    • 17044364059 scopus 로고    scopus 로고
    • Breast-feeding and the use of human milk
    • American Academy of Pediatrics. Breast-feeding and the use of human milk. Pediatrics 115 (2005) 96-506
    • (2005) Pediatrics , vol.115 , pp. 96-506
    • American Academy of Pediatrics1
  • 2
    • 0037125113 scopus 로고    scopus 로고
    • Modeling the kinetics of whey protein hydrolysis brought about by enzymes from Cynara cadunculus
    • Barros R.M., and Malcata F.X. Modeling the kinetics of whey protein hydrolysis brought about by enzymes from Cynara cadunculus. Journal of Agricultural and Food Chemistry 50 (2002) 4347-4356
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , pp. 4347-4356
    • Barros, R.M.1    Malcata, F.X.2
  • 3
    • 3242790859 scopus 로고    scopus 로고
    • A kinetic model for hydrolysis of whey proteins by cardosin A extracted from Cynara cardunculus
    • Barros R.M., and Malcata F.X. A kinetic model for hydrolysis of whey proteins by cardosin A extracted from Cynara cardunculus. Food Chemistry 88 (2004) 351-359
    • (2004) Food Chemistry , vol.88 , pp. 351-359
    • Barros, R.M.1    Malcata, F.X.2
  • 4
    • 33746307095 scopus 로고    scopus 로고
    • Studies on ultrafiltration of casein whey using a rotating disk module: effects of pH and membrane disk rotation
    • Bhattacharjee S., Ghosh S., Datta S., and Bhattacharjee C. Studies on ultrafiltration of casein whey using a rotating disk module: effects of pH and membrane disk rotation. Desalination 195 (2006) 95-108
    • (2006) Desalination , vol.195 , pp. 95-108
    • Bhattacharjee, S.1    Ghosh, S.2    Datta, S.3    Bhattacharjee, C.4
  • 5
    • 84897601233 scopus 로고    scopus 로고
    • Enzyme reaction
    • Wiley-VCH, Weinheim, Germany pp. 7-164
    • Bisswanger H. Enzyme reaction. In Practical enzymology (2004), Wiley-VCH, Weinheim, Germany pp. 7-164
    • (2004) In Practical enzymology
    • Bisswanger, H.1
  • 6
    • 0642311539 scopus 로고    scopus 로고
    • Milk proteins modification to improve functional and biological properties
    • Taylor S.L. (Ed), Academic Press, New York, NY, USA
    • Chobert J.-M. Milk proteins modification to improve functional and biological properties. In: Taylor S.L. (Ed). Advances in food and nutrition research Vol. 47 (2003), Academic Press, New York, NY, USA 1-71
    • (2003) Advances in food and nutrition research , vol.47 , pp. 1-71
    • Chobert, J.-M.1
  • 7
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • Church F.C., Swaisgood H.E., Porter D.H., and Catignani G.L. Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science 66 (1983) 1219-1227
    • (1983) Journal of Dairy Science , vol.66 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3    Catignani, G.L.4
  • 8
    • 0001823720 scopus 로고
    • Structure-function relationship of food proteins
    • Hettiarachchy N.S., and Ziegler G.R. (Eds), Marcel Decker, New York, NY, USA
    • Damodaran S. Structure-function relationship of food proteins. In: Hettiarachchy N.S., and Ziegler G.R. (Eds). Protein functionality in food systems (1994), Marcel Decker, New York, NY, USA 1-37
    • (1994) Protein functionality in food systems , pp. 1-37
    • Damodaran, S.1
  • 9
    • 0015101812 scopus 로고
    • Studies on the interactions between purified bovine caseins and alkaline-earth-metal ions
    • Dickson I.R., and Perkins D.J. Studies on the interactions between purified bovine caseins and alkaline-earth-metal ions. Biochemical Journal 124 (1971) 235-240
    • (1971) Biochemical Journal , vol.124 , pp. 235-240
    • Dickson, I.R.1    Perkins, D.J.2
  • 10
    • 0033990823 scopus 로고    scopus 로고
    • Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: a comparison with cow's and buffalo milk proteins
    • Elagamy E.I. Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: a comparison with cow's and buffalo milk proteins. Food Chemistry 68 (2000) 227-232
    • (2000) Food Chemistry , vol.68 , pp. 227-232
    • Elagamy, E.I.1
  • 12
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: production and functionality
    • Korhonen H., and Pihlanto A. Bioactive peptides: production and functionality. International Dairy Journal 16 (2006) 945-960
    • (2006) International Dairy Journal , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 13
    • 0024368356 scopus 로고
    • Enzymic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula
    • Li Chan E., and Nakai S. Enzymic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula. Journal of Dairy Research 56 (1989) 381-390
    • (1989) Journal of Dairy Research , vol.56 , pp. 381-390
    • Li Chan, E.1    Nakai, S.2
  • 14
    • 0027465258 scopus 로고
    • Bradford protein assay and the transition from an insoluble to a soluble dye complex: effects of sodium dodecyl sulphate and other additives
    • Marshall T., and Williams K.M. Bradford protein assay and the transition from an insoluble to a soluble dye complex: effects of sodium dodecyl sulphate and other additives. Journal of Biochemical and Biophysical Methods 26 (1993) 237-240
    • (1993) Journal of Biochemical and Biophysical Methods , vol.26 , pp. 237-240
    • Marshall, T.1    Williams, K.M.2
  • 15
    • 0036118984 scopus 로고    scopus 로고
    • Proteolytic activity of Staphylococcus xylosus strains on pork myofibrillar and sarcoplasmic proteins and use of selected strains in the production of `Naples type' salami
    • Mauriello G., Casaburi A., and Villani F. Proteolytic activity of Staphylococcus xylosus strains on pork myofibrillar and sarcoplasmic proteins and use of selected strains in the production of `Naples type' salami. Journal of Applied Microbiology 92 (2002) 482-490
    • (2002) Journal of Applied Microbiology , vol.92 , pp. 482-490
    • Mauriello, G.1    Casaburi, A.2    Villani, F.3
  • 16
    • 84987368873 scopus 로고
    • Physicochemical and dynamic properties of caseins modified by chemical phosphorylation
    • Medina A.L., Colas B., Le Meste M., Renaudet I., and Lorient D. Physicochemical and dynamic properties of caseins modified by chemical phosphorylation. Journal of Food Science 57 (1992) 617-621
    • (1992) Journal of Food Science , vol.57 , pp. 617-621
    • Medina, A.L.1    Colas, B.2    Le Meste, M.3    Renaudet, I.4    Lorient, D.5
  • 17
    • 0032076817 scopus 로고    scopus 로고
    • Overview on milk protein-derived peptides
    • Meisel H. Overview on milk protein-derived peptides. International Dairy Journal 8 (1998) 363-373
    • (1998) International Dairy Journal , vol.8 , pp. 363-373
    • Meisel, H.1
  • 18
    • 22544468502 scopus 로고    scopus 로고
    • Biochemical properties of peptides encrypted in bovine milk protein
    • Meisel H. Biochemical properties of peptides encrypted in bovine milk protein. Current Medical Chemistry 12 (2005) 1905-1919
    • (2005) Current Medical Chemistry , vol.12 , pp. 1905-1919
    • Meisel, H.1
  • 20
    • 6944241742 scopus 로고    scopus 로고
    • Release of short and proline-rich antihypertensive peptides from casein hydrolysate with an Aspergillus oryzae protease
    • Mizuno S., Nishimura S., Matsuura K., Gotou T., and Yamamoto N. Release of short and proline-rich antihypertensive peptides from casein hydrolysate with an Aspergillus oryzae protease. Journal of Dairy Science 87 (2004) 3183-3188
    • (2004) Journal of Dairy Science , vol.87 , pp. 3183-3188
    • Mizuno, S.1    Nishimura, S.2    Matsuura, K.3    Gotou, T.4    Yamamoto, N.5
  • 22
    • 0033801179 scopus 로고    scopus 로고
    • Hydrolysis of ovine, caprine and bovine whey proteins by trypsin and pepsin
    • Pintado M.E., and Malcata F.X. Hydrolysis of ovine, caprine and bovine whey proteins by trypsin and pepsin. Bioprocess Engineering 23 (2000) 275-282
    • (2000) Bioprocess Engineering , vol.23 , pp. 275-282
    • Pintado, M.E.1    Malcata, F.X.2
  • 24
    • 0037292844 scopus 로고    scopus 로고
    • Product distribution of casein tryptic hydrolysis based on HPSEC analysis and molecular mechanism
    • Qi W., He Z., and Shi D. Product distribution of casein tryptic hydrolysis based on HPSEC analysis and molecular mechanism. Chemical Engineering Science 58 (2003) 767-775
    • (2003) Chemical Engineering Science , vol.58 , pp. 767-775
    • Qi, W.1    He, Z.2    Shi, D.3
  • 25
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analytical Biochemistry 166 (1987) 368-379
    • (1987) Analytical Biochemistry , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 27
    • 33748104885 scopus 로고    scopus 로고
    • Bioactive peptide in ovine and caprine cheeselike systems prepared with proteases from Cynara cardunculus
    • Silva S.V., Pihlanto A., and Malcata F.X. Bioactive peptide in ovine and caprine cheeselike systems prepared with proteases from Cynara cardunculus. Journal of Dairy Science 89 (2006) 3336-3344
    • (2006) Journal of Dairy Science , vol.89 , pp. 3336-3344
    • Silva, S.V.1    Pihlanto, A.2    Malcata, F.X.3
  • 28
    • 0030983488 scopus 로고    scopus 로고
    • Reviews of methods for the analysis of protein hydrolysates
    • Silvestre M.P.C. Reviews of methods for the analysis of protein hydrolysates. Food Chemistry 60 (1997) 263-271
    • (1997) Food Chemistry , vol.60 , pp. 263-271
    • Silvestre, M.P.C.1
  • 29
    • 0035994521 scopus 로고    scopus 로고
    • Advances in the role of a plant coagulant (Cynara cardunculus) in vitro and during ripening of cheese from several milk species
    • Sousa M.J., and Malcata F.X. Advances in the role of a plant coagulant (Cynara cardunculus) in vitro and during ripening of cheese from several milk species. Lait 82 (2002) 151-170
    • (2002) Lait , vol.82 , pp. 151-170
    • Sousa, M.J.1    Malcata, F.X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.