메뉴 건너뛰기




Volumn 99, Issue 2-3, 2011, Pages 187-190

Effect of heat treatment on lactoperoxidase activity in camel milk: A comparison with bovine lactoperoxidase

Author keywords

Bovine milk; Camel milk; Lactoperoxidase; Thermal stability

Indexed keywords

BOVINAE;

EID: 79961208286     PISSN: 09214488     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.smallrumres.2011.04.007     Document Type: Article
Times cited : (24)

References (24)
  • 1
    • 0001430290 scopus 로고    scopus 로고
    • Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk
    • Anema S.G., McKenna A.B. Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. J. Agric. Food Chem. 1996, 44:422-428.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 422-428
    • Anema, S.G.1    McKenna, A.B.2
  • 2
    • 79961208298 scopus 로고
    • Dairy products. Determination of ash content. Standard 945.46
    • Association of Official Analytical Chemists, Washington, DC, USA AOAC
    • AOAC Dairy products. Determination of ash content. Standard 945.46. Official Methods of Analysis 1995, Association of Official Analytical Chemists, Washington, DC, USA.
    • (1995) Official Methods of Analysis
  • 3
    • 0033081533 scopus 로고    scopus 로고
    • Contribution of the lactoperoxidase system to the keeping quality of pasteurised milk
    • Barrett N.E., Grandison A.S., Lewis M.J. Contribution of the lactoperoxidase system to the keeping quality of pasteurised milk. J. Dairy Res. 1999, 66:73-80.
    • (1999) J. Dairy Res. , vol.66 , pp. 73-80
    • Barrett, N.E.1    Grandison, A.S.2    Lewis, M.J.3
  • 5
    • 33748304355 scopus 로고    scopus 로고
    • Lactoperoxidase: from catalytic mechanism to practical applications
    • Boots J.W., Floris R. Lactoperoxidase: from catalytic mechanism to practical applications. Int. Dairy J. 2006, 16:1272-1276.
    • (2006) Int. Dairy J. , vol.16 , pp. 1272-1276
    • Boots, J.W.1    Floris, R.2
  • 7
    • 33645407624 scopus 로고    scopus 로고
    • Indigenous enzymes in milk: overview and historical aspects. Part 1
    • Fox P.F., Kelly A.L. Indigenous enzymes in milk: overview and historical aspects. Part 1. Int. Dairy J. 2006, 16:500-516.
    • (2006) Int. Dairy J. , vol.16 , pp. 500-516
    • Fox, P.F.1    Kelly, A.L.2
  • 8
    • 0001588557 scopus 로고
    • Use of milk enzymes as indices of heat treatment
    • Griffiths M. Use of milk enzymes as indices of heat treatment. J. Food Prot. 1986, 49:696-705.
    • (1986) J. Food Prot. , vol.49 , pp. 696-705
    • Griffiths, M.1
  • 9
    • 0030163309 scopus 로고    scopus 로고
    • Preservation of raw milk by activation of the natural lactoperoxidase systems
    • Haddadin M.S., Ibrahim S.A., Robinson R.K. Preservation of raw milk by activation of the natural lactoperoxidase systems. Food Cont. 1996, 7:149-152.
    • (1996) Food Cont. , vol.7 , pp. 149-152
    • Haddadin, M.S.1    Ibrahim, S.A.2    Robinson, R.K.3
  • 10
    • 0033961193 scopus 로고    scopus 로고
    • A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin
    • Hendrix T., Griko Y.V., Privalov P.L. A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophys. Chem. 2000, 84:27-34.
    • (2000) Biophys. Chem. , vol.84 , pp. 27-34
    • Hendrix, T.1    Griko, Y.V.2    Privalov, P.L.3
  • 11
    • 0001393284 scopus 로고
    • Isolation and properties of lactoperoxidase from bovine milk
    • Hernandez M., Van Markwijk B., Vreeman H. Isolation and properties of lactoperoxidase from bovine milk. Neth. Milk Dairy J. 1990, 44:213-231.
    • (1990) Neth. Milk Dairy J. , vol.44 , pp. 213-231
    • Hernandez, M.1    Van Markwijk, B.2    Vreeman, H.3
  • 12
    • 33751302231 scopus 로고
    • Milk. Determination of total solids
    • International Dairy Federation, Brussels, Belgium, IDF
    • IDF Milk. Determination of total solids. International Dairy Federation Standard 70 1970, International Dairy Federation, Brussels, Belgium.
    • (1970) International Dairy Federation Standard 70
  • 13
    • 33751288314 scopus 로고
    • Milk. Determination of the nitrogen (Kjeldahl method) and calculation of the crude protein content
    • International Dairy Federation, Brussels, Belgium IDF
    • IDF Milk. Determination of the nitrogen (Kjeldahl method) and calculation of the crude protein content. International Dairy Federation Standard 20B 1993, International Dairy Federation, Brussels, Belgium.
    • (1993) International Dairy Federation Standard 20B
  • 15
    • 0034492989 scopus 로고    scopus 로고
    • Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications
    • Kussendrager K.D., van Hooijdonk A.C.M. Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 2000, 84:S19-S25.
    • (2000) Br. J. Nutr. , vol.84
    • Kussendrager, K.D.1    van Hooijdonk, A.C.M.2
  • 16
    • 21844451900 scopus 로고    scopus 로고
    • Effect of the lactoperoxidase system against three major causal agents of disease in mangoes
    • Le Nguyen D.D., Ducamp M.N., Dornier M., Montet D., Loiseau G. Effect of the lactoperoxidase system against three major causal agents of disease in mangoes. J. Food Prot. 2005, 68:1497-1500.
    • (2005) J. Food Prot. , vol.68 , pp. 1497-1500
    • Le Nguyen, D.D.1    Ducamp, M.N.2    Dornier, M.3    Montet, D.4    Loiseau, G.5
  • 17
    • 0035524079 scopus 로고    scopus 로고
    • Inactivation kinetics of alkaline phosphatase and lactoperoxidase, and denaturation of β-lactoglobulin in raw milk under isothermal and dynamic temperature conditions
    • Ludikhuyze L.R., Claeys W.L., Hendrickx M.E. Inactivation kinetics of alkaline phosphatase and lactoperoxidase, and denaturation of β-lactoglobulin in raw milk under isothermal and dynamic temperature conditions. J. Dairy Res. 2001, 68:625-637.
    • (2001) J. Dairy Res. , vol.68 , pp. 625-637
    • Ludikhuyze, L.R.1    Claeys, W.L.2    Hendrickx, M.E.3
  • 18
    • 0037286903 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine lactoperoxidase activity in skim milk: kinetic and thermodynamic analysis
    • Marin E., Sanches L., Perez M.D., Puyol P., Calvo M. Effect of heat treatment on bovine lactoperoxidase activity in skim milk: kinetic and thermodynamic analysis. J. Food Sci. 2003, 68:89-93.
    • (2003) J. Food Sci. , vol.68 , pp. 89-93
    • Marin, E.1    Sanches, L.2    Perez, M.D.3    Puyol, P.4    Calvo, M.5
  • 19
    • 0025676440 scopus 로고
    • Quantitative, standardized assays for determining the concentrations of bovine lactoperoxidase, human salivary peroxidase, and human myeloperoxidase
    • Pruitt K.M., Kamau D.N., Miller K., Mansson-Rahemtulla B., Rahemtulla F. Quantitative, standardized assays for determining the concentrations of bovine lactoperoxidase, human salivary peroxidase, and human myeloperoxidase. Anal. Biochem. 1990, 191:278-286.
    • (1990) Anal. Biochem. , vol.191 , pp. 278-286
    • Pruitt, K.M.1    Kamau, D.N.2    Miller, K.3    Mansson-Rahemtulla, B.4    Rahemtulla, F.5
  • 21
    • 63449119347 scopus 로고    scopus 로고
    • Effect of heat treatment on buffalo (Bubalus bubalis) lactoperoxidase activity in raw milk
    • Tayefi-Nasrabadi H., Asadpour R. Effect of heat treatment on buffalo (Bubalus bubalis) lactoperoxidase activity in raw milk. J. Boil. Sci. 2008, 8:1310-1315.
    • (2008) J. Boil. Sci. , vol.8 , pp. 1310-1315
    • Tayefi-Nasrabadi, H.1    Asadpour, R.2
  • 22
    • 2342570869 scopus 로고    scopus 로고
    • Effects of a lactoperoxidase-thiocyanate-hydrogen peroxide system on Salmonella enteritidis in animal or vegetable foods
    • Touch V., Hayakawa S., Yamada S., Kaneko S. Effects of a lactoperoxidase-thiocyanate-hydrogen peroxide system on Salmonella enteritidis in animal or vegetable foods. Int. J. Food Microbiol. 2004, 93:175-183.
    • (2004) Int. J. Food Microbiol. , vol.93 , pp. 175-183
    • Touch, V.1    Hayakawa, S.2    Yamada, S.3    Kaneko, S.4
  • 23
    • 33751274194 scopus 로고    scopus 로고
    • Effect of heat treatment on lactoperoxidase activity in caprine milk
    • Trujillo A.J., Pozo P.I., Guamis B. Effect of heat treatment on lactoperoxidase activity in caprine milk. Small Ruminant Res. 2007, 67:243-246.
    • (2007) Small Ruminant Res. , vol.67 , pp. 243-246
    • Trujillo, A.J.1    Pozo, P.I.2    Guamis, B.3
  • 24
    • 77952323466 scopus 로고    scopus 로고
    • Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH
    • Zelent B., Sharp K.A., Vanderkooi J.M. Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH. Biochim. Biophys. Acta. 2010, 1804:1508-1515.
    • (2010) Biochim. Biophys. Acta. , vol.1804 , pp. 1508-1515
    • Zelent, B.1    Sharp, K.A.2    Vanderkooi, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.