Journal of Dairy Science
Volume 90, Issue 11 , Pages 4954-4965 , November 2007

Profile of Gelatinolytic Capacity of Raw Goat Milk and the Implications for Milk Quality

  • W.Y. Chen

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • ,
  • M.H. Weng

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • ,
  • S.E. Chen

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • ,
  • H.C. Peh

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • ,
  • W.B. Liu

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • ,
  • T.C. Yu

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • ,
  • M.C. Huang

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • ,
  • M.T. Chen

      Affiliations

    • Department of Bioindustry Technology, Da Yeh University, Chung Hwwa 515, Taiwan, Republic of China
    • ,
  • H. Nagahata

      Affiliations

    • Department of Animal Health, School of Veterinary Medicine, Rakuno Gakuen University, Ebetsu, Hokkaido 069-8501, Japan
    • ,
  • C.J. Chang

      Affiliations

    • Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
    • Corresponding Author InformationCorresponding author.

Received 17 May 2007 ,Accepted 25 June 2007.

References 

  1. Attaie R, Richter RL. Size distribution of fat globules in goat milk. J. Dairy Sci. 2000;83:940–944
  2. Cuzner ML, Opdenakker G. Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system. J. Neuroimmunol. 1999;94:1–14
  3. Denhard M, Claus R, Munz O, Weiler U. Course of epidermal growth factor (EGF) and insulin-like growth factor I (IGF-I) in mammary secretion of goat during end-pregnancy and early lactation. J. Vet. Med. A Physiol. Pathol. Clin. Med. 2000;47:533–540
  4. Donadio AC, Durand S, Remedi MM, Frede S, Ceschin DG, Genti-Raimondi S, et al. Evaluation of stromal metalloproteinases and vascular endothelial growth factors in a spontaneous metastasis model. Exp. Mol. Pathol. 2005;79:259–264
  5. Droke EA, Paape MJ, Di Carlo AL. Prevalence of high somatic cell counts in bulk tank goat milk. J. Dairy Sci. 1993;76:1035–1039
  6. Fantuz F, Polidori F, Cheli F, Baldi A. Plasminogen activation system in goat milk and its relation with composition and coagulation properties. J. Dairy Sci. 2001;84:1786–1790
  7. Faurschou M, Borregaard N. Neutrophil granules and secretory vesicles in inflammation. Microbes Infect. 2003;14:1317–1327
  8. Haddadi K, Moussaoui F, Hebia I, Laurent F, Le Roux Y. E. coli proteolytic activity in milk and casein breakdown. Reprod. Nutr. Dev. 2005;45:485–496
  9. Hayes KD, Nielsen SS. Plasmin levels in fresh milk whey and commercial whey protein products. J. Dairy Sci. 2000;83:387–394
  10. Jouglin M, Robert C, Valette J, Gavard F, Quintin-Colonna F, Denoix J. Metalloproteinases and tumor necrosis factor-alpha activities in synovial fluids of horses: Correlation with articular cartilage alterations. Vet. Res. 2000;31:507–515
  11. Laemmli UK. Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature. 1970;227:680–685
  12. Larsen LB, Rasmussen MD, Bjerring M, Nielson JH. Proteases and protein degradation in milk from cows infected with Streptococcus uberis. Int. Dairy J. 2004;14:899–907
  13. Leitner G, Merin U, Silanikove N. Changes in milk composition as affected by subclinical mastitis in goats. J. Dairy Sci. 2004;87:1719–1726
  14. Le Roux Y, Colin O, Laurent F. Proteolysis in samples of quarter milk with varying somatic cell counts. 1. Comparison of some indicators of endogenous proteolysis in milk. J. Dairy Sci. 1995;78:1289–1297
  15. Le Roux Y, Laurent F, Moussaoui F. Polymorphonuclear proteolytic activity and milk composition change. Vet. Res. 2003;34:9–45
  16. Luengo C, Sanchez A, Corrales JC, Fernandez C, Contreras A. Influence of intramammary infection and non-infection factors on somatic cell counts in dairy goats. J. Dairy Res. 2004;71:169–174
  17. Makowski GS, Ramsby ML. Calibrating gelatin zymograms with human gelatinase standards. Anal. Biochem. 1996;236:353–356
  18. Makowski GS, Ramsby ML. Zymographic analysis of latent and activated forms of matrix metalloproteinase-2 and -9 in synovial fluid: Correlation to polymorphonuclear leukocyte infiltration and in response to infection. Clin. Chim. Acta. 2003;329:77–81
  19. Mora-Gutierrez A, Kumosinski TF, Farrell HM. Quantification of αs1-casein in goat milk from French-Alpine and Anglo-Nubian breeds using reversed-phase high performance liquid chromatography. J. Dairy Sci. 1991;74:3303–3307
  20. Moroni P, Pisoni G, Savoini G, van Lier E, Acuña S, Damián JP, et al. Influence of estrus of dairy goats on somatic cell count, milk traits, and sex steroid receptors in the mammary gland. J. Dairy Sci. 2007;90:790–797
  21. Moussaoui F, Laurent F, Girardet JM, Humbert G, Gaillard JL, Le Roux Y. Characterization and proteolytic origins of specific peptides appearing during lipopolysaccharide experimental mastitis. J. Dairy Sci. 2003;86:1163–1170
  22. Muehlherr JE, Zweifel C, Corti S, Blanco JE, Stephan R. Microbiological quality of raw goat's and ewe's bulk-tank milk in Switzerland. J. Dairy Sci. 2003;86:3849–3856
  23. Nielsen SS. Plasmin system and microbial proteases in milk: Characteristics, roles, and relationship. J. Agric. Food Chem. 2002;50:6628–6634
  24. Paape MJ, Poutrel B, Contreras A, Marco JC, Capuco AV. Milk somatic cells and lactation in small ruminants. J. Dairy Sci. 2001;84(E Suppl.):E237–E244
  25. Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodeling. Nat. Rev. Mol. Cell Biol. 2007;8:221–233
  26. Politis I. Plasminogen activator system: Implications for mammary cell growth and involution. J. Dairy Sci. 1996;79:1097–1107
  27. Prosser C, Steiwagen K, Cummins R, Guerin P, Gill N, Miline C. Reduction of heat-induced gastrointestinal hyper-permeability in rats by bovine colostrums and goat milk powders. J. Appl. Physiol. 2004;96:650–654
  28. Rabot A, Sinowatz F, Berisha B, Meyer HHD, Schams D. Expression and localization of extracellular matrix-degrading proteinases and their inhibitors in the bovine mammary gland during development, function, and involution. J. Dairy Sci. 2007;90:740–748
  29. Raulo SM, Sorsa T, Tervahartiala T, Latvanen T, Pirila E, Hirvonen J, et al. Increase in milk metalloproteinase activity and vascular permeability in bovine endotoxin-induced and naturally occurring Escherichia coli mastitis. Vet. Immunol. Immunopathol. 2002;85:137–145
  30. Renner M. Milk and Milk Products in Human Nutrition, Vdkswirtsch. Germany: Verlag GmbH, Munich; 1982;
  31. Salama AAK, Caja G, Such X, Casals R, Albanell E. Effect of pregnancy and extended lactation on milk production in dairy goats milked once daily. J. Dairy Sci. 2005;88:3894–3904
  32. Sanchez A, Sierra D, Luengo C, Corrales JC, Morales CT, Contreras A, et al. Influence of storage and preservation on Fossomatic cell count and composition of goat milk. J. Dairy Sci. 2006;88:3095–3100
  33. SAS Institute. SAS/STAT User's Guide. Release 6.12.. Cary, NC: SAS Institute Inc.; 2003;
  34. Sordillo LM, Nickerson SC. Morphologic changes in the bovine mammary gland during involution and lactogenesis. Am. J. Vet. Res. 1988;49:1112–1120
  35. Tian SZ, Chang CJ, Chiang CC, Peh HC, Huang MC, Lee JW, et al. Comparison of morphology, viability and function between blood and milk neutrophils from peak lactating goats. Can. J. Vet. Res. 2005;69:39–45
  36. Van den Steen PE, Dubois B, Nelissen I, Rudd MP, Dwek RA, Opdenakker G. Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit. Rev. Biochem. Mol. Biol. 2002;37:375–536
  37. Van Hekken DL, Tunick MH, Park YW. Rheological and proteolytic proterties of Monterey Jack goat's milk cheese during aging. J. Agric. Food Chem. 2004;52:5372–5377
  38. Weng MH, Chang CJ, Chen YW, Chou WK, Peh HC, Huang MC, et al. Contribution of somatic cell-associated activation of plasminogen to caseinolysis within the goat mammary gland. J. Dairy Sci. 2006;89:2025–2037
  39. Wu FY, Tsao PH, Wang DC, Lin S, Wu JS, Cheng YK. Factors affecting growth factor activity in goat milk. J. Dairy Sci. 2006;89:1951–1955
  40. Zeng SS, Escobar EN, Popham T. Daily variations in somatic cell count, composition, and production of Alpine goat milk. Small Rumin. Res. 1997;26:253–260

PII: S0022-0302(07)71963-X

doi: 10.3168/jds.2007-0366

Journal of Dairy Science
Volume 90, Issue 11 , Pages 4954-4965 , November 2007

Article Tools

* Image Usage & Resolution