메뉴 건너뛰기




Volumn 63, Issue 1, 2010, Pages 16-31

Indigenous enzymatic activities in ovine and caprine milks

Author keywords

Caprine milk; Indigenous enzymes; Ovine milk

Indexed keywords

BOVINAE; CAPRA; OVIS;

EID: 75149153475     PISSN: 1364727X     EISSN: 14710307     Source Type: Journal    
DOI: 10.1111/j.1471-0307.2009.00552.x     Document Type: Review
Times cited : (38)

References (131)
  • 2
    • 3142703063 scopus 로고    scopus 로고
    • Effects of somatic cell count and stage of lactation on the plasmin activity and cheese-making properties of ewe milk
    • Albenzio M, Caroprese M, Santillo A, Marino R, Taibi L Sevi A (2004) Effects of somatic cell count and stage of lactation on the plasmin activity and cheese-making properties of ewe milk. Journal of Dairy Science 87 533 542.
    • (2004) Journal of Dairy Science , vol.87 , pp. 533-542
    • Albenzio, M.1    Caroprese, M.2    Santillo, A.3    Marino, R.4    Taibi, L.5    Sevi, A.6
  • 3
    • 14044275239 scopus 로고    scopus 로고
    • Proteolytic patterns and plasmin activity in ewes' milk as affected by somatic cell count and stage of lactation
    • Albenzio M, Caroprese M, Santillo A, Marino R, Muscio A Sevi A (2005) Proteolytic patterns and plasmin activity in ewes' milk as affected by somatic cell count and stage of lactation. Journal of Dairy Science 72 86 92.
    • (2005) Journal of Dairy Science , vol.72 , pp. 86-92
    • Albenzio, M.1    Caroprese, M.2    Santillo, A.3    Marino, R.4    Muscio, A.5    Sevi, A.6
  • 5
    • 33846999914 scopus 로고    scopus 로고
    • Effects of ventilation rate and of dietary protein level in an intensive dairy sheep system on the features of Canestrano Pugliese cheese
    • Albenzio M, Santillo A, Caroprese M, Marino R, Annicchiarico G Sevi A (2007) Effects of ventilation rate and of dietary protein level in an intensive dairy sheep system on the features of Canestrano Pugliese cheese. Journal of Dairy Research 74 26 33.
    • (2007) Journal of Dairy Research , vol.74 , pp. 26-33
    • Albenzio, M.1    Santillo, A.2    Caroprese, M.3    Marino, R.4    Annicchiarico, G.5    Sevi, A.6
  • 8
    • 0035432594 scopus 로고    scopus 로고
    • Analysis time and lactation stage influence of lactoperoxidase system components in dairy ewe milk
    • Althaus R L, Molina M P, Rodríguez M Fernández N (2001) Analysis time and lactation stage influence of lactoperoxidase system components in dairy ewe milk. Journal of Dairy Science 84 1829 1835.
    • (2001) Journal of Dairy Science , vol.84 , pp. 1829-1835
    • Althaus, R.L.1    Molina, M.P.2    Rodríguez, M.3    Fernández, N.4
  • 9
    • 75149120768 scopus 로고
    • Bovine milk acid phosphatase. II. Binding to casein substrates and heat-inactivation studies
    • Andrews A T (1974) Bovine milk acid phosphatase. II. Binding to casein substrates and heat-inactivation studies. Journal of Dairy Research 42 401 417.
    • (1974) Journal of Dairy Research , vol.42 , pp. 401-417
    • Andrews, A.T.1
  • 10
    • 84971947684 scopus 로고
    • The acid phosphatases of bovine leucocytes, plasma and the milk of healthy and mastitic cows
    • Andrews A T Alichanidis E (1975a) The acid phosphatases of bovine leucocytes, plasma and the milk of healthy and mastitic cows. Journal of Dairy Research 42 391 400.
    • (1975) Journal of Dairy Research , vol.42 , pp. 391-400
    • Andrews, A.T.1    Alichanidis, E.2
  • 12
    • 0008013620 scopus 로고
    • Alkaline phosphatase activity of sheep's milk and some factors affecting
    • Anifantakis E M Rosakis P S (1983) Alkaline phosphatase activity of sheep's milk and some factors affecting. Egyptian Journal of Dairy Science 11 173 182.
    • (1983) Egyptian Journal of Dairy Science , vol.11 , pp. 173-182
    • Anifantakis, E.M.1    Rosakis, P.S.2
  • 13
    • 75149167182 scopus 로고    scopus 로고
    • Determination of alkaline phosphatise activity levels in milk from indigenous Portuguese ewe and goat breeds by the fluorometric method
    • International Dairy Federation Bulletin 351, p 34. IDF. ed. Brussels. International Dairy Federation
    • Assis G, Roseiro I B Barbosa M (2000) Determination of alkaline phosphatise activity levels in milk from indigenous Portuguese ewe and goat breeds by the fluorometric method. In Proceedings of Development Strategy for the Sheep and Goat Dairy Sector, International Dairy Federation Bulletin 351, p 34. IDF ed., Brussels: International Dairy Federation.
    • (2000) Proceedings of Development Strategy for the Sheep and Goat Dairy Sector
    • Assis, G.1    Roseiro, I.B.2    Barbosa, M.3
  • 14
    • 1642405513 scopus 로고    scopus 로고
    • Goat's milk xanthine oxidoreductase is grossly deficient in molybdenum
    • Atmani D, Benboubetra M Harrison R (2004) Goat's milk xanthine oxidoreductase is grossly deficient in molybdenum. Journal of Dairy Research 71 7 13.
    • (2004) Journal of Dairy Research , vol.71 , pp. 7-13
    • Atmani, D.1    Benboubetra, M.2    Harrison, R.3
  • 16
    • 0024669966 scopus 로고
    • Paracellular leakage of lipoprotein lipase across the mammary epithelium of the goat
    • Azzara C D Dimick P S (1989) Paracellular leakage of lipoprotein lipase across the mammary epithelium of the goat. Journal of Dairy Science 72 1159 1168.
    • (1989) Journal of Dairy Science , vol.72 , pp. 1159-1168
    • Azzara, C.D.1    Dimick, P.S.2
  • 19
    • 33645795905 scopus 로고    scopus 로고
    • Why does the increase of plasmin worsen the coagulation properties pf milk in dairy sheep?
    • Battacone G, Cannas E A, Mazzette A, Dimauro C Enne G (2005) Why does the increase of plasmin worsen the coagulation properties pf milk in dairy sheep? Italian Journal of Animal Science 4 (Suppl. 2) 342 344.
    • (2005) Italian Journal of Animal Science , vol.4 , Issue.SUPPL. 2 , pp. 342-344
    • Battacone, G.1    Cannas, E.A.2    Mazzette, A.3    Dimauro, C.4    Enne, G.5
  • 20
    • 3142575498 scopus 로고    scopus 로고
    • Physicochemical and kinetic properties of purified sheep's milk xanthine oxidoreductase
    • Benboubetra M, Baghiani A, Atmani D Harrison R (2004) Physicochemical and kinetic properties of purified sheep's milk xanthine oxidoreductase. Journal of Dairy Science 87 1580 1584.
    • (2004) Journal of Dairy Science , vol.87 , pp. 1580-1584
    • Benboubetra, M.1    Baghiani, A.2    Atmani, D.3    Harrison, R.4
  • 22
    • 0018989524 scopus 로고
    • Free and membrane-bound xanthine oxidase in bovine milk during cooling and heating
    • Bhavadasam M K Ganguli N G (1980) Free and membrane-bound xanthine oxidase in bovine milk during cooling and heating. Journal of Dairy Science 63 362 367.
    • (1980) Journal of Dairy Science , vol.63 , pp. 362-367
    • Bhavadasam, M.K.1    Ganguli, N.G.2
  • 24
    • 0027013659 scopus 로고
    • Purification and properties of alkaline phosphatase in the lactating mammary gland
    • Bingham E W, Garrer K Powlem D (1992) Purification and properties of alkaline phosphatase in the lactating mammary gland. Journal of Dairy Science 75 3394 3401.
    • (1992) Journal of Dairy Science , vol.75 , pp. 3394-3401
    • Bingham, E.W.1    Garrer, K.2    Powlem, D.3
  • 25
    • 0000997859 scopus 로고
    • The lactoperoxidase/thiocyanate/hydrogen peroxide system as a temporary preservative for raw milk in developing countries
    • Björck L, Claesson O Schulthess W (1979) The lactoperoxidase/ thiocyanate/hydrogen peroxide system as a temporary preservative for raw milk in developing countries. Milchwissenschaft 34 726 729.
    • (1979) Milchwissenschaft , vol.34 , pp. 726-729
    • Björck, L.1    Claesson, O.2    Schulthess, W.3
  • 26
    • 0034329936 scopus 로고    scopus 로고
    • Rapid Communication: Nucleotide sequence of the ovine lipoprotein lipase cDNA
    • Bonnet M C, Leroux Y, Chilliard Y Martin P (2000) Rapid Communication: nucleotide sequence of the ovine lipoprotein lipase cDNA. Journal of Animal Science 78 2994 2995.
    • (2000) Journal of Animal Science , vol.78 , pp. 2994-2995
    • Bonnet, M.C.1    Leroux, Y.2    Chilliard, Y.3    Martin, P.4
  • 27
    • 0035638063 scopus 로고    scopus 로고
    • Influence of the nature of alpine pastures on plasmin activity, fatty acid and volatile compound composition of milk
    • Bugaud C, Buchin S, Coulon J B, Hauwuy A Dupont D (2001) Influence of the nature of alpine pastures on plasmin activity, fatty acid and volatile compound composition of milk. Le Lait 81 401 414.
    • (2001) Le Lait , vol.81 , pp. 401-414
    • Bugaud, C.1    Buchin, S.2    Coulon, J.B.3    Hauwuy, A.4    Dupont, D.5
  • 28
    • 33645382159 scopus 로고    scopus 로고
    • Effect of thermal treatment on the activation of bovine plasminogen
    • Burbrink C N Hayes K D (2006) Effect of thermal treatment on the activation of bovine plasminogen. International Dairy Journal 16 580 585.
    • (2006) International Dairy Journal , vol.16 , pp. 580-585
    • Burbrink, C.N.1    Hayes, K.D.2
  • 29
    • 34547658157 scopus 로고    scopus 로고
    • Contribution of macrophages to proteolysis and plasmin activity in ewe bulk milk
    • DOI 10.3168/jds.2006-691
    • Caroprese M, Marzano A, Schena L, Marino R, Santillo A Albenzio M (2007) Contribution of macro phages to proteolysis and plasmin activity in ewe bulk milk. Journal of Dairy Science 90 2767 2772. (Pubitemid 350049668)
    • (2007) Journal of Dairy Science , vol.90 , Issue.6 , pp. 2767-2772
    • Caroprese, M.1    Marzano, A.2    Schena, L.3    Marino, R.4    Santillo, A.5    Albenzio, M.6
  • 30
    • 47149117438 scopus 로고    scopus 로고
    • Effect of milking interval on milk secretion and mammary tight junction permeability in dairy ewes
    • Castillo V, Such X, Caja G, Casals R, Albanell E Salama A A K (2008) Effect of milking interval on milk secretion and mammary tight junction permeability in dairy ewes. Journal of Dairy Science 91 2610 2619.
    • (2008) Journal of Dairy Science , vol.91 , pp. 2610-2619
    • Castillo, V.1    Such, X.2    Caja, G.3    Casals, R.4    Albanell, E.5    Salama, A.A.K.6
  • 33
    • 0542404094 scopus 로고    scopus 로고
    • Alkaline phosphatase, acid phosphatase, lactoperoxidase and lipoprotein lipase activities in industrial ewe's milk and cheese
    • Chávarri F, Santistebam A, Virto M de Renobales M (1998) Alkaline phosphatase, acid phosphatase, lactoperoxidase and lipoprotein lipase activities in industrial ewe's milk and cheese. Journal of Agricultural and Food Chemistry 46 2926 2932.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 2926-2932
    • Chávarri, F.1    Santistebam, A.2    Virto, M.3    De Renobales, M.4
  • 34
    • 0022819784 scopus 로고
    • Effect of stage of lactation, stage of pregnancy, milk yield and herd management on seasonal variation in spontaneous lipolysis in bovine milk
    • Chazal M P Chilliard Y (1986) Effect of stage of lactation, stage of pregnancy, milk yield and herd management on seasonal variation in spontaneous lipolysis in bovine milk. Journal of Dairy Research 53 529 538.
    • (1986) Journal of Dairy Research , vol.53 , pp. 529-538
    • Chazal, M.P.1    Chilliard, Y.2
  • 35
    • 0039029167 scopus 로고
    • Variations physiologiques des activités lipasiques et de la lipolyse spontanée dans les laits de vache de chèvre et de femme: Revue bibliographique (suite)
    • Chilliard Y (1982) Variations physiologiques des activités lipasiques et de la lipolyse spontanée dans les laits de vache de chèvre et de femme: revue bibliographique (suite). Le Lait 62 126 154.
    • (1982) Le Lait , vol.62 , pp. 126-154
    • Chilliard, Y.1
  • 37
    • 0041807789 scopus 로고    scopus 로고
    • A review of nutritional and physiological factors affecting goat milk synthesis and lipolysis
    • Chilliard Y, Ferlay A, Rouel J Lamberet G (2003) A review of nutritional and physiological factors affecting goat milk synthesis and lipolysis. Journal of Dairy Science 86 1751 1770.
    • (2003) Journal of Dairy Science , vol.86 , pp. 1751-1770
    • Chilliard, Y.1    Ferlay, A.2    Rouel, J.3    Lamberet, G.4
  • 38
    • 0026677272 scopus 로고
    • Alkaline phosphatase activity and pyridoxal phosphate concentrations in the milk of various species
    • Coburn S P, Mahuren J D, Pauly T A, Ericson K L Townsend D W (1992) Alkaline phosphatase activity and pyridoxal phosphate concentrations in the milk of various species. The Journal of Nutrition 122 2348 2353.
    • (1992) The Journal of Nutrition , vol.122 , pp. 2348-2353
    • Coburn, S.P.1    Mahuren, J.D.2    Pauly, T.A.3    Ericson, K.L.4    Townsend, D.W.5
  • 39
    • 0142260532 scopus 로고    scopus 로고
    • Lipolysis and free fatty acid catabolism in cheese: A review of the current knowledge
    • Collins Y F, McSweeney P L.H Wilkinson M G (2003) Lipolysis and free fatty acid catabolism in cheese: a review of the current knowledge. International Dairy Journal 13 841 866.
    • (2003) International Dairy Journal , vol.13 , pp. 841-866
    • Collins, Y.F.1    McSweeney, P.L.H.2    Wilkinson, M.G.3
  • 40
    • 0742305574 scopus 로고    scopus 로고
    • Hydrolysis of bovine caseins by cathepsin B, a cysteine proteinase indigenous to milk
    • Considine T, Healy A, Kelly A L McSweeney P L H (2004) Hydrolysis of bovine caseins by cathepsin B, a cysteine proteinase indigenous to milk. International Dairy Journal 14 117 124.
    • (2004) International Dairy Journal , vol.14 , pp. 117-124
    • Considine, T.1    Healy, A.2    Kelly, A.L.3    McSweeney, P.L.H.4
  • 41
    • 33645406061 scopus 로고    scopus 로고
    • An investigation of the plasmin-plasminogen system in caprine milk and cheese
    • Cortellino G, Locci F Rampilli M (2006) An investigation of the plasmin-plasminogen system in caprine milk and cheese. International Dairy Journal, 16 619 622.
    • (2006) International Dairy Journal , vol.16 , pp. 619-622
    • Cortellino, G.1    Locci, F.2    Rampilli, M.3
  • 42
    • 0023357779 scopus 로고
    • Selenium content and distribution in human, cow and goat milk
    • Debski B, Picciano M F Milner J A (1987) Selenium content and distribution in human, cow and goat milk. Journal of Nutrition 117 1091 1097.
    • (1987) Journal of Nutrition , vol.117 , pp. 1091-1097
    • Debski, B.1    Picciano, M.F.2    Milner, J.A.3
  • 43
    • 33645412967 scopus 로고    scopus 로고
    • Lipoprotein lipase and lipolysis in milk
    • Deeth H C (2006) Lipoprotein lipase and lipolysis in milk. International Dairy Journal 16 555 562.
    • (2006) International Dairy Journal , vol.16 , pp. 555-562
    • Deeth, H.C.1
  • 44
    • 0004787425 scopus 로고
    • Factors governing the susceptibility of milk to spontaneous lipolysis
    • pp. International Dairy Federation Bulletin No 86. IDF. ed. Brussels. International Dairy Federation
    • Deeth H C Fitz-Gerald C H (1975) Factors governing the susceptibility of milk to spontaneous lipolysis. In Proceedings of the lipolysis symposium, pp 24 34, International Dairy Federation Bulletin No 86, IDF ed. Brussels: International Dairy Federation.
    • (1975) Proceedings of the Lipolysis Symposium , pp. 24-34
    • Deeth, H.C.1    Fitz-Gerald, C.H.2
  • 45
    • 0000136846 scopus 로고    scopus 로고
    • Influence des variants AA et FF de la caséine γs1 caprine sur le rendement fromager et les charactéristiques des fromages
    • Delacroix-Buchet A, Degas C, Lamembert G Vassal L (1996) Influence des variants AA et FF de la caséine γs1 caprine sur le rendement fromager et les charactéristiques des fromages. Le Lait 76 217 21.
    • (1996) Le Lait , vol.76 , pp. 217-241
    • Delacroix-Buchet, A.1    Degas, C.2    Lamembert, G.3    Vassal, L.4
  • 47
    • 0035432217 scopus 로고    scopus 로고
    • Plasminogen activation system in goat milk and its relation with composition and coagulation properties
    • Fantuz F, Polidori F, Cheli F Baldi A (2001) Plasminogen activation system in goat milk and its relation with composition and coagulation properties. Journal of Dairy Science 84 1786 1790.
    • (2001) Journal of Dairy Science , vol.84 , pp. 1786-1790
    • Fantuz, F.1    Polidori, F.2    Cheli, F.3    Baldi, A.4
  • 48
    • 33645387601 scopus 로고    scopus 로고
    • Other enzymes
    • Part A, pp. Fox, P. F. McSweeney, P. L H. eds. New York, USA. Kluwer Academic/Plenum
    • Farkye N Y (2003) Other Enzymes. In Advanced Dairy Chemistry: Vol. 1 Proteins, 3rd edn, Part A, pp. 571 603. Fox P F, McSweeney P L H, eds. New York, USA: Kluwer Academic/Plenum.
    • (2003) Advanced Dairy Chemistry: Vol. 1 Proteins, 3rd Edn , pp. 571-603
    • Farkye, N.Y.1
  • 50
    • 0036698594 scopus 로고    scopus 로고
    • Variations of lactoperoxidase activity and thiocyanate content in cows' and goats' milk throughout lactation
    • Fonteh F A, Grandison A S Lewis M J (2002) Variations of lactoperoxidase activity and thiocyanate content in cows' and goats' milk throughout lactation. Journal of Dairy Research 69 401 409.
    • (2002) Journal of Dairy Research , vol.69 , pp. 401-409
    • Fonteh, F.A.1    Grandison, A.S.2    Lewis, M.J.3
  • 51
    • 33645407624 scopus 로고    scopus 로고
    • Indigenous enzymes in milk: Overview and historical aspects-Part 1
    • Fox P F Kelly A L (2006a) Indigenous enzymes in milk: overview and historical aspects-Part 1. International Dairy Journal 16 500 516.
    • (2006) International Dairy Journal , vol.16 , pp. 500-516
    • Fox, P.F.1    Kelly, A.L.2
  • 52
    • 33645393430 scopus 로고    scopus 로고
    • Indigenous enzymes in milk: Overview and historical aspects-Part 2
    • Fox P F Kelly A L (2006b) Indigenous enzymes in milk: overview and historical aspects-Part 2. International Dairy Journal 16 517 532.
    • (2006) International Dairy Journal , vol.16 , pp. 517-532
    • Fox, P.F.1    Kelly, A.L.2
  • 53
    • 1642402107 scopus 로고
    • Factors affecting the apparent activity and heat sensitivity of xanthine oxidase in milk
    • Gudnason G V Shipe W F (1962) Factors affecting the apparent activity and heat sensitivity of xanthine oxidase in milk. Journal of Dairy Science 45 1440 1448.
    • (1962) Journal of Dairy Science , vol.45 , pp. 1440-1448
    • Gudnason, G.V.1    Shipe, W.F.2
  • 55
    • 0027570828 scopus 로고
    • Release of volatile branched-chain and other fatty acids from ruminant milk fats by various lipases
    • Ha J K Lindsay R C (1993) Release of volatile branched-chain and other fatty acids from ruminant milk fats by various lipases. Journal of Dairy Science 76 677 690.
    • (1993) Journal of Dairy Science , vol.76 , pp. 677-690
    • Ha, J.K.1    Lindsay, R.C.2
  • 56
    • 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 (1996) Preservation of raw milk by activation of the natural lactoperoxidase systems. Food Control 7 149 152.
    • (1996) Food Control , vol.7 , pp. 149-152
    • Haddadin, M.S.1    Ibrahim, S.A.2    Robinson, R.K.3
  • 57
    • 18444364526 scopus 로고    scopus 로고
    • Collaborative evaluation of a fluorometric method for measuring alkaline phosphatase activity in cow's, sheep's and goat's milk
    • Harding F Garry E (2005) Collaborative evaluation of a fluorometric method for measuring alkaline phosphatase activity in cow's, sheep's and goat's milk. Journal of Food Protection 68 1047 1053.
    • (2005) Journal of Food Protection , vol.68 , pp. 1047-1053
    • Harding, F.1    Garry, E.2
  • 59
    • 0037105296 scopus 로고    scopus 로고
    • Structure and function of xanthine oxidoreductase. Where are we now?
    • Harrison R (2002b) Structure and function of xanthine oxidoreductase. Where are we now? Free Radical Biology and Medicine 33 774 797.
    • (2002) Free Radical Biology and Medicine , vol.33 , pp. 774-797
    • Harrison, R.1
  • 60
    • 33645391515 scopus 로고    scopus 로고
    • Milk xanthine oxidase: Properties and physiological roles
    • Harrison R (2006) Milk xanthine oxidase: properties and physiological roles. International Dairy Journal 16 546 554.
    • (2006) International Dairy Journal , vol.16 , pp. 546-554
    • Harrison, R.1
  • 62
    • 0019034154 scopus 로고
    • Occurrence and consequence of superoxide dismutase in milk products: A review
    • Hicks C L (1980) Occurrence and consequence of superoxide dismutase in milk products: a review. Journal of Dairy Science 63 1199 1204.
    • (1980) Journal of Dairy Science , vol.63 , pp. 1199-1204
    • Hicks, C.L.1
  • 63
    • 0018461360 scopus 로고
    • Heat inactivation of superoxide dismutase in bovine milk
    • Hicks C L, Bucy J Stofer W (1979) Heat inactivation of superoxide dismutase in bovine milk. Journal of Dairy Science 62 529 532.
    • (1979) Journal of Dairy Science , vol.62 , pp. 529-532
    • Hicks, C.L.1    Bucy, J.2    Stofer, W.3
  • 64
    • 0031991665 scopus 로고    scopus 로고
    • Milk catalase activity as an indicator of thermalization treatments used in the manufacture of Cheddar cheese
    • Hirvi Y Griffiths M W (1998) Milk catalase activity as an indicator of thermalization treatments used in the manufacture of Cheddar cheese. Journal of Dairy Science 81 338 345.
    • (1998) Journal of Dairy Science , vol.81 , pp. 338-345
    • Hirvi, Y.1    Griffiths, M.W.2
  • 67
    • 33846816146 scopus 로고
    • Isoenzymes of catalase in goat milk
    • Dairy Science Abstracts
    • Ito O Akuzawa R (1984) Isoenzymes of catalase in goat milk. Japanese Journal of Zootechnical Science 55, 220 226. Dairy Science Abstracts.
    • (1984) Japanese Journal of Zootechnical Science , vol.55 , pp. 220-226
    • Ito, O.1    Akuzawa, R.2
  • 68
    • 0024121078 scopus 로고
    • Use of N-acetyl-beta-glucosaminidase to detect teat can inflammations
    • Kaartinen L Jensen N E (1988) Use of N-acetyl-beta-glucosaminidase to detect teat can inflammations. Journal of Dairy Science 55 603 607.
    • (1988) Journal of Dairy Science , vol.55 , pp. 603-607
    • Kaartinen, L.1    Jensen, N.E.2
  • 69
    • 0742296737 scopus 로고    scopus 로고
    • Indigenous proteinases in milk
    • Part A, pp. Fox, P. F. McSweeney, P. L H. eds. New York, USA. Kluwer Academic/Plenum
    • Kelly A L McSweeney P L H (2003) Indigenous proteinases in milk. In Advanced Dairy Chemistry: Vol. 1 Proteins, 3rd edn, Part A, pp. 495 522. Fox P F, McSweeney P L H, eds. New York, USA: Kluwer Academic/Plenum.
    • (2003) Advanced Dairy Chemistry: Vol. 1 Proteins, 3rd Edn , pp. 495-522
    • Kelly, A.L.1    McSweeney, P.L.H.2
  • 70
    • 33645418473 scopus 로고    scopus 로고
    • Indigenous proteolytic enzymes in milk: A brief overview of the present stage of knowledge
    • Kelly A L, O'Flaherty F Fox P F (2006) Indigenous proteolytic enzymes in milk: a brief overview of the present stage of knowledge. International Dairy Journal 16 563 572.
    • (2006) International Dairy Journal , vol.16 , pp. 563-572
    • Kelly, A.L.1    O'Flaherty, F.2    Fox, P.F.3
  • 72
    • 51949115371 scopus 로고    scopus 로고
    • Assessment of the colorimetric and fluorometric assays for alkaline phosphatase activity in cow's, goat's and sheep's milk
    • Klotz V, Hill A, Warriner K, Griffiths M Odumeru J (2008) Assessment of the colorimetric and fluorometric assays for alkaline phosphatase activity in cow's, goat's and sheep's milk. Journal of Food Protection 71 1884 1888.
    • (2008) Journal of Food Protection , vol.71 , pp. 1884-1888
    • Klotz, V.1    Hill, A.2    Warriner, K.3    Griffiths, M.4    Odumeru, J.5
  • 73
    • 0034492989 scopus 로고    scopus 로고
    • Lactoperoxidase: Physicochemical properties, occurrence, mechanism of action and applications
    • Kussendrager K D Van Hooijdonk A C M (2000) Lactoperoxidase: physicochemical properties, occurrence, mechanism of action and applications. British Journal of Nutrition 84 519 525.
    • (2000) British Journal of Nutrition , vol.84 , pp. 519-525
    • Kussendrager, K.D.1    Van Hooijdonk, A.C.M.2
  • 76
    • 1642526598 scopus 로고    scopus 로고
    • Changes in milk composition as affected by subclinical mastitis in goats
    • Leitner G, Merin U Silanikove N (2004b) Changes in milk composition as affected by subclinical mastitis in goats. Journal of Dairy Science 87 1719 1726. (Pubitemid 38893301)
    • (2004) Journal of Dairy Science , vol.87 , Issue.6 , pp. 1719-1726
    • Leitner, G.1    Merin, U.2    Silanikove, N.3
  • 77
    • 33645420920 scopus 로고    scopus 로고
    • Interactions between bacteria type, proteolysis of casein and physico-chemical properties of bovine milk
    • Leitner G, Krifucks O, Merin U, Lavi Y Silanikove N (2006) Interactions between bacteria type, proteolysis of casein and physico-chemical properties of bovine milk. International Dairy Journal 16 648 654.
    • (2006) International Dairy Journal , vol.16 , pp. 648-654
    • Leitner, G.1    Krifucks, O.2    Merin, U.3    Lavi, Y.4    Silanikove, N.5
  • 79
    • 0025811817 scopus 로고
    • Lysozyme and γ-lactalbumin: Structure function and interrelationships
    • McKenzie H A White F H Jr. (1991) Lysozyme and γ-lactalbumin: structure function and interrelationships. Advances in Protein Chemistry 41 173 315.
    • (1991) Advances in Protein Chemistry , vol.41 , pp. 173-315
    • McKenzie, H.A.1    White Jr., F.H.2
  • 80
    • 84985400033 scopus 로고
    • The lactoperoxidase system in ewe's milk: Levels of lactoperoxidase and thiocyanate
    • Medina M, Gaya P Nuňez M (1989) The lactoperoxidase system in ewe's milk: levels of lactoperoxidase and thiocyanate. Letters in Applied Microbiology 8 147 149.
    • (1989) Letters in Applied Microbiology , vol.8 , pp. 147-149
    • Medina, M.1    Gaya, P.2    Nuňez, M.3
  • 81
    • 0002182861 scopus 로고
    • The composition of goat milk as affected by nutritional parameters
    • Merin U, Rosental I Maltz E (1988) The composition of goat milk as affected by nutritional parameters. Milchwissenschaft 43 363 365.
    • (1988) Milchwissenschaft , vol.43 , pp. 363-365
    • Merin, U.1    Rosental, I.2    Maltz, E.3
  • 82
    • 0023408856 scopus 로고
    • Ribonuclease activity and isoenzymes in raw and processed cows' milk and infant formulas
    • Meyer D H, Kunin A S, Maddalena J Meyer W L (1987) Ribonuclease activity and isoenzymes in raw and processed cows' milk and infant formulas. Journal of Dairy Science 70 1797 1803.
    • (1987) Journal of Dairy Science , vol.70 , pp. 1797-1803
    • Meyer, D.H.1    Kunin, A.S.2    Maddalena, J.3    Meyer, W.L.4
  • 83
    • 48749096575 scopus 로고    scopus 로고
    • Effect of high-pressure treatment at various temperatures on indigenous proteolytic enzymes and whey protein denaturation in bovine milk
    • Moatsou G, Bakopanos C, Katharios D, Katsaros G, Kandarakis I, Taoukis P Politis I (2008a) Effect of high-pressure treatment at various temperatures on indigenous proteolytic enzymes and whey protein denaturation in bovine milk. Journal of Dairy Research 75 262 269.
    • (2008) Journal of Dairy Research , vol.75 , pp. 262-269
    • Moatsou, G.1    Bakopanos, C.2    Katharios, D.3    Katsaros, G.4    Kandarakis, I.5    Taoukis, P.6    Politis, I.7
  • 84
    • 50849117504 scopus 로고    scopus 로고
    • Effect of high-pressure treatment at various temperatures on activity of indigenous enzymes and denaturation of whey proteins in ovine milk
    • Moatsou G, Katsaros G, Bakopanos C, Kandarakis I, Taoukis P Politis I (2008b) Effect of high-pressure treatment at various temperatures on activity of indigenous enzymes and denaturation of whey proteins in ovine milk. International Dairy Journal 18 1119 1125.
    • (2008) International Dairy Journal , vol.18 , pp. 1119-1125
    • Moatsou, G.1    Katsaros, G.2    Bakopanos, C.3    Kandarakis, I.4    Taoukis, P.5    Politis, I.6
  • 86
    • 64449084824 scopus 로고    scopus 로고
    • The influence of lactoperoxidase, heat and low pH on survival of acid-adapted and non-adapted Escherichia coli O157:H7 in goat milk
    • Parry-Hanson A, Jooste P J Buys E M (2009) The influence of lactoperoxidase, heat and low pH on survival of acid-adapted and non-adapted Escherichia coli O157:H7 in goat milk. International Dairy Journal 19 417 421.
    • (2009) International Dairy Journal , vol.19 , pp. 417-421
    • Parry-Hanson, A.1    Jooste, P.J.2    Buys, E.M.3
  • 87
    • 85005586916 scopus 로고
    • Heat exchanger performance: γ-glutamyl transpeptidase assay as a heat treatment indicator for dairy products
    • Patel S S Wilbey R A (1989) Heat exchanger performance: γ-glutamyl transpeptidase assay as a heat treatment indicator for dairy products. Journal of the Society of Dairy Technology 42 79 80.
    • (1989) Journal of the Society of Dairy Technology , vol.42 , pp. 79-80
    • Patel, S.S.1    Wilbey, R.A.2
  • 88
  • 91
    • 0026874913 scopus 로고
    • Distribution of plasminogen and plasmin in fractions of bovine milk
    • Politis I, Barbano D M Gorewit R C (1992) Distribution of plasminogen and plasmin in fractions of bovine milk. Journal of Dairy Science 75 1402 1410.
    • (1992) Journal of Dairy Science , vol.75 , pp. 1402-1410
    • Politis, I.1    Barbano, D.M.2    Gorewit, R.C.3
  • 93
    • 0036237749 scopus 로고    scopus 로고
    • The urokinase-plasminogen activator system in ovine macro phages and neutrophils
    • Politis I, Bizelis I Rogdakis E (2002) The urokinase-plasminogen activator system in ovine macro phages and neutrophils. Small Ruminant Research 44 17 23.
    • (2002) Small Ruminant Research , vol.44 , pp. 17-23
    • Politis, I.1    Bizelis, I.2    Rogdakis, E.3
  • 94
    • 4043170541 scopus 로고    scopus 로고
    • Effect of vitamin e supplementation on neutrophil function, milk composition and plasmin activity in dairy cows in a commercial herd
    • Politis I, Bizelis I, Tsiaras A Baldi A (2004) Effect of vitamin E supplementation on neutrophil function, milk composition and plasmin activity in dairy cows in a commercial herd. Journal of Dairy Research 71 273 278.
    • (2004) Journal of Dairy Research , vol.71 , pp. 273-278
    • Politis, I.1    Bizelis, I.2    Tsiaras, A.3    Baldi, A.4
  • 95
    • 33645407152 scopus 로고    scopus 로고
    • Effect of heat treatment on the activity of inhibitors of plasmin and plasminogen activators in milk
    • Prado B M, Sombers S E, Ismail B Hayes K D (2006) Effect of heat treatment on the activity of inhibitors of plasmin and plasminogen activators in milk. International Dairy Journal 16 593 599.
    • (2006) International Dairy Journal , vol.16 , pp. 593-599
    • Prado, B.M.1    Sombers, S.E.2    Ismail, B.3    Hayes, K.D.4
  • 96
    • 27644557199 scopus 로고    scopus 로고
    • Lactoperoxidase
    • Part A, pp. Fox, P. F. McSweeney, P. L H. eds. New York, USA. Kluwer Academic/Plenum
    • Pruitt K M (2003) Lactoperoxidase. In Advanced Dairy Chemistry: Vol. 1 Proteins, 3rd edn, Part A, pp. 563 570. Fox P F, McSweeney P L H, eds. New York, USA: Kluwer Academic/Plenum.
    • (2003) Advanced Dairy Chemistry: Vol. 1 Proteins, 3rd Edn , pp. 563-570
    • Pruitt, K.M.1
  • 99
  • 101
    • 0033028171 scopus 로고    scopus 로고
    • Relationships between lactoperoxidase system components in Creole goat milk
    • Saad de Schoos S, Oliver G Fernandez F M (1999) Relationships between lactoperoxidase system components in Creole goat milk. Small Ruminant Research 32 69 75.
    • (1999) Small Ruminant Research , vol.32 , pp. 69-75
    • Saad De Schoos, S.1    Oliver, G.2    Fernandez, F.M.3
  • 102
    • 33750733947 scopus 로고    scopus 로고
    • Evaluation of a chemiluminescence method for measuring alkaline phosphates activity in whole milk of multiple species and bovine dairy drinks: Interlaboratory studies
    • Salter R S Fitchen J (2006) Evaluation of a chemiluminescence method for measuring alkaline phosphates activity in whole milk of multiple species and bovine dairy drinks: interlaboratory studies. Journal of AOAC International 89 1061 1070.
    • (2006) Journal of AOAC International , vol.89 , pp. 1061-1070
    • Salter, R.S.1    Fitchen, J.2
  • 104
    • 0036001712 scopus 로고    scopus 로고
    • Enhancing keeping quality of raw cow's, sheep's and goat's milks by activation of the lactoperoxidase system
    • Savci Z, Sezgin E Yildirim Z (2002) Enhancing keeping quality of raw cow's, sheep's and goat's milks by activation of the lactoperoxidase system. Milchwissenschaft 57 13 15.
    • (2002) Milchwissenschaft , vol.57 , pp. 13-15
    • Savci, Z.1    Sezgin, E.2    Yildirim, Z.3
  • 105
    • 0033834668 scopus 로고    scopus 로고
    • Evaluation of spectrophotometric and fluorometric methods for alkaline phosphatase activity determination in ewe's milk
    • Scintu M F, Daga E Ledda A (2000) Evaluation of spectrophotometric and fluorometric methods for alkaline phosphatase activity determination in ewe's milk. Journal of Food Protection 63 1258 1261.
    • (2000) Journal of Food Protection , vol.63 , pp. 1258-1261
    • Scintu, M.F.1    Daga, E.2    Ledda, A.3
  • 106
    • 1842817575 scopus 로고    scopus 로고
    • Antibacterial activity of lactoperoxidase system against food-borne pathogens in Saanen and South African Indigenous goat milk
    • Seifu E, Buys E M, Donkin E F Petzer I-M (2004) Antibacterial activity of lactoperoxidase system against food-borne pathogens in Saanen and South African Indigenous goat milk. Food Control 15 447 452.
    • (2004) Food Control , vol.15 , pp. 447-452
    • Seifu, E.1    Buys, E.M.2    Donkin, E.F.3    Petzer, I.-M.4
  • 107
    • 16244397401 scopus 로고    scopus 로고
    • Significance of the lactoperoxidase system in dairy industry and its potential application: A review
    • Seifu E, Buys E M Donkin E F (2005) Significance of the lactoperoxidase system in dairy industry and its potential application: a review. Trends in Food Science and Technology 16 137 154.
    • (2005) Trends in Food Science and Technology , vol.16 , pp. 137-154
    • Seifu, E.1    Buys, E.M.2    Donkin, E.F.3
  • 110
    • 33645389264 scopus 로고    scopus 로고
    • A preliminary study on the role of alkaline phosphatase in cheese ripening
    • Shakeel-Ur-Rehman, Farkye N Y Yim B (2006) A preliminary study on the role of alkaline phosphatase in cheese ripening. International Dairy Journal 16 697 700.
    • (2006) International Dairy Journal , vol.16 , pp. 697-700
    • Shakeel-Ur-Rehman1    Farkye, N.Y.2    Yim, B.3
  • 111
    • 65349186686 scopus 로고    scopus 로고
    • Activity and thermal stability of indigenous enzymes in cow, buffalo and goat milk
    • Sharma R, Kaur S, Rajput Y S Kumar R (2009) Activity and thermal stability of indigenous enzymes in cow, buffalo and goat milk. Milchwissenschaft 64 173 175.
    • (2009) Milchwissenschaft , vol.64 , pp. 173-175
    • Sharma, R.1    Kaur, S.2    Rajput, Y.S.3    Kumar, R.4
  • 112
    • 34447647821 scopus 로고    scopus 로고
    • Distribution of xanthine oxidase and xanthine dehydrogenase activity in bovine milk: Physiological and technological implications
    • Silanikove N Shapiro F (2007) Distribution of xanthine oxidase and xanthine dehydrogenase activity in bovine milk: physiological and technological implications. International Dairy Journal 17 1188 1194.
    • (2007) International Dairy Journal , vol.17 , pp. 1188-1194
    • Silanikove, N.1    Shapiro, F.2
  • 113
    • 21344464457 scopus 로고    scopus 로고
    • Interrelationships between the activities of the plasmin system system in goats and sheep experiencing subclinical mastitis, casein degradation and milk yield
    • Silanikove N, Shapiro F, Leitner G Merin U (2004) Interrelationships between the activities of the plasmin system system in goats and sheep experiencing subclinical mastitis, casein degradation and milk yield. South African Journal of Animal Sciences 34 (Suppl. 1) 192 194.
    • (2004) South African Journal of Animal Sciences , vol.34 , Issue.SUPPL. 1 , pp. 192-194
    • Silanikove, N.1    Shapiro, F.2    Leitner, G.3    Merin, U.4
  • 114
    • 0040032893 scopus 로고
    • Flavor of goat's milk: A review of studies on the sources of its variations
    • Skjevdal T (1979) Flavor of goat's milk: a review of studies on the sources of its variations. Livestock Production Science 6 397 405.
    • (1979) Livestock Production Science , vol.6 , pp. 397-405
    • Skjevdal, T.1
  • 116
    • 0023497690 scopus 로고
    • Hydrolysis of bovine and caprine milk fat globules by lipoprotein lipase. Effects of heparin and of skim milk on lipase distribution and on lipolysis
    • Sundheim G Bengtsson-Olivecrona G (1987) Hydrolysis of bovine and caprine milk fat globules by lipoprotein lipase. Effects of heparin and of skim milk on lipase distribution and on lipolysis. Journal of Dairy Science 70 2467 2475.
    • (1987) Journal of Dairy Science , vol.70 , pp. 2467-2475
    • Sundheim, G.1    Bengtsson-Olivecrona, G.2
  • 117
    • 35748939062 scopus 로고    scopus 로고
    • Factors affecting the plasmin-plasminogen system in milk obtained from three Greek Dairy sheep breeds with major differences in milk production capacity
    • Theodorou G, Kominakis A, Rogdakis E Politis I (2007) Factors affecting the plasmin-plasminogen system in milk obtained from three Greek Dairy sheep breeds with major differences in milk production capacity. Journal of Dairy Science 90 3263 3269.
    • (2007) Journal of Dairy Science , vol.90 , pp. 3263-3269
    • Theodorou, G.1    Kominakis, A.2    Rogdakis, E.3    Politis, I.4
  • 118
    • 33751274194 scopus 로고    scopus 로고
    • Effect of heat treatment on lactoperoxidase activity in caprine milk
    • Trujillo A J, Pozo P I Guamis B (2007) Effect of heat treatment on lactoperoxidase activity in caprine milk. Small Ruminant Research 67 243 246.
    • (2007) Small Ruminant Research , vol.67 , pp. 243-246
    • Trujillo, A.J.1    Pozo, P.I.2    Guamis, B.3
  • 119
    • 21344482701 scopus 로고
    • The effect of ewe milk lactoperoxidase system on Pseudomonas fluoresence growth casein breakdown, peptide formation and milk coagulation characteristics
    • Uceda R, Guillen AM, Gaya P, Medina M Nuňez M (1994) The effect of ewe milk lactoperoxidase system on Pseudomonas fluoresence growth casein breakdown, peptide formation and milk coagulation characteristics. Milchwissenschaft 49 139 143.
    • (1994) Milchwissenschaft , vol.49 , pp. 139-143
    • Uceda, R.1    Guillen, A.M.2    Gaya, P.3    Medina, M.4    Nuňez, M.5
  • 123
    • 33847080732 scopus 로고    scopus 로고
    • Kinetics in thermal activation of alkaline phospatase in bovine and caprine milk and buffer
    • Wilińska A, Bryjak J, Illeová V Polakovič M (2007) Kinetics in thermal activation of alkaline phospatase in bovine and caprine milk and buffer. International Dairy Journal 17 579 586.
    • (2007) International Dairy Journal , vol.17 , pp. 579-586
    • Wilińska, A.1    Bryjak, J.2    Illeová, V.3    Polakovič, M.4
  • 124
    • 0036164130 scopus 로고    scopus 로고
    • Relationships of somatic cell count, physical, chemical and enzymatic properties to the bacterial standard plate count in dairy goat milk
    • Ying C, Wang H-T Hsu J-T (2002) Relationships of somatic cell count, physical, chemical and enzymatic properties to the bacterial standard plate count in dairy goat milk. Livestock Production Science 74 63 77.
    • (2002) Livestock Production Science , vol.74 , pp. 63-77
    • Ying, C.1    Wang, H.-T.2    Hsu, J.-T.3
  • 127
    • 67349240163 scopus 로고    scopus 로고
    • Protein composition of caprine milk fat globule membrane
    • Zamora A, Guamis B Trujillo A J (2009) Protein composition of caprine milk fat globule membrane. Small Ruminant Research 82 122 129.
    • (2009) Small Ruminant Research , vol.82 , pp. 122-129
    • Zamora, A.1    Guamis, B.2    Trujillo, A.J.3
  • 129
    • 0026127319 scopus 로고
    • Influence of breed, animal and days of lactation on lactoperoxidase system components in goat milk
    • Zapico P, Gaya P, De Paz M, Nuňez M Medina M (1991) Influence of breed, animal and days of lactation on lactoperoxidase system components in goat milk. Journal of Dairy Science 74 783 787.
    • (1991) Journal of Dairy Science , vol.74 , pp. 783-787
    • Zapico, P.1    Gaya, P.2    De Paz, M.3    Nuňez, M.4    Medina, M.5
  • 131
    • 0000144401 scopus 로고
    • Effect of parity and milk production on somatic cell count, standard plate count and composition of goat milk
    • Zeng S S Escobar E N (1995) Effect of parity and milk production on somatic cell count, standard plate count and composition of goat milk. Small Ruminant Research 17 269 274.
    • (1995) Small Ruminant Research , vol.17 , pp. 269-274
    • Zeng, S.S.1    Escobar, E.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.