Hostname: page-component-78c5997874-lj6df Total loading time: 0 Render date: 2024-11-20T05:42:35.846Z Has data issue: false hasContentIssue false
  • English
  • Français

Haptoglobin and serum amyloid A in bulk tank milk in relation to raw milk quality

Published online by Cambridge University Press:  17 September 2009

Maria Åkerstedt ,
Karin Persson Waller  and
Åse Sternesjö
Maria Åkerstedt*
Affiliation:
Department of Food Science, Swedish University of Agricultural Sciences, SE-750 07 Uppsala, Sweden
Karin Persson Waller
Affiliation:
Department of Animal Health and Antimicrobial Strategies, National Veterinary Institute, SE-751 89 Uppsala, Sweden Department of Clinical Sciences, Swedish University of Agricultural Sciences, SE-750 07 Uppsala, Sweden
Åse Sternesjö
Affiliation:
Department of Food Science, Swedish University of Agricultural Sciences, SE-750 07 Uppsala, Sweden
*
*For correspondence; e-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

The aim of the present study was to evaluate relationships between the presence of the two major bovine acute phase proteins haptoglobin (Hp) and serum amyloid A (SAA) and raw milk quality parameters in bulk tank milk samples. Hp and SAA have been suggested as specific markers of mastitis but recently also as markers for raw milk quality. Since mastitis has detrimental effects on milk quality, it is important to investigate whether the presence of Hp or SAA indicates such changes in the composition and properties of the milk. Bulk tank milk samples (n=91) were analysed for Hp, SAA, total protein, casein, whey protein, proteolysis, fat, lactose, somatic cell count and coagulating properties. Samples with detectable levels of Hp had lower casein content, casein number and lactose content, but higher proteolysis than samples without Hp. Samples with detectable levels of SAA had lower casein number and lactose content, but higher whey protein content than samples without SAA. The presence of acute phase proteins in bulk tank milk is suggested as an indicator for unfavourable changes in the milk composition, e.g. protein quality, due to udder health disturbances, with economical implications for the dairy industry.

Keywords

Acute phase proteinsmilk qualitybulk tank milk
Type
Research Article
Information
Journal of Dairy Research , Volume 76 , Issue 4 , November 2009 , pp. 483 - 489
Copyright
Copyright © Proprietors of Journal of Dairy Research 2009

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Åkerstedt, M, Björck, L, Persson Waller, K & Sternesjö, Å 2006 Biosensor assay for determination of haptoglobin in bovine milk. Journal of Dairy Research 73 299–305CrossRefGoogle ScholarPubMed
Åkerstedt, M, Persson Waller, K & Sternesjö, Å 2007 Haptoglobin and serum amyloid A in relation to the somatic cell count at quarter, cow composite and bulk tank milk samples. Journal of Dairy Research 74 198–203CrossRefGoogle Scholar
Åkerstedt, M, Persson Waller, K, Bach Larsen, L, Forsbäck, L & Sternesjö, Å 2008 Relationship between haptoglobin and serum amyloid A in relation to milk quality. International Dairy Journal 18 669–674CrossRefGoogle Scholar
Auldist, MJ, Coats, S, Sutherland, BJ, Mayes, JJ, McDowell, GH & Rogers, GL 1996 Effects of somatic cell count and stage of lactation on raw milk composition and the yield and quality of cheddar cheese. Journal of Dairy Research 63 269–280CrossRefGoogle ScholarPubMed
Barbano, DM, Rasmussen, RR & Lynch, JM 1991 Influence of milk somatic cell count and milk age on cheese yield. Journal of Dairy Science 74 369–388CrossRefGoogle Scholar
Barbano, DM, Ma, Y & Santos, MV 2006 Influence of raw milk quality on fluid milk shelf life. Journal of Dairy Science 89 (E.Suppl.):E15–E19CrossRefGoogle ScholarPubMed
De Noni, I, Pellegrino, L, Cattaneo, S & Resmini, P 2007 HPLC of proteose peptones for evaluating ageing of packaged pasteurized milk. International Dairy Journal 17 12–19CrossRefGoogle Scholar
Eaton, JW, Brandt, P, Mahoney, JR & Lee, JT 1982 Haptoglobin: A natural bacteriostat. Science 215 691–693CrossRefGoogle ScholarPubMed
Eckersall, PD, Young, FJ, McComb, C, Hogarth, CJ, Safi, S, Weber, A, McDonald, T, Nolan, AM & Fitzpatrick, JL 2001 Acute phase proteins in serum and milk from dairy cows with clinical mastitis. Veterinary Record 148 35–41CrossRefGoogle ScholarPubMed
Eckersall, PD 2004 The time is right for acute phase proteins assay. Veterinary Journal 168 3–5CrossRefGoogle Scholar
Eckersall, PD, Young, FJ, Nolan, AM, Knight, CH, McComb, C, Waterston, MM, Hogarth, CJ, Scott, EM & Fitzpatrick, JL 2006 Acute phase proteins in bovine milk in an experimental model of Staphylococcus aureus subclinical mastitis. Journal of Dairy Science 89 1488–1501CrossRefGoogle Scholar
Grönlund, U, Hulten, C, Eckersall, PD, Hogarth, C & Persson Waller, K 2003 Haptoglobin and serum amyloid A in milk and serum during acute and chronic experimentally induced Staphylococcus aureus mastitis. Journal of Dairy Research 70 379–386CrossRefGoogle ScholarPubMed
Grönlund, U, Hallén Sandgren, C & Persson Waller, K 2005 Haptoglobin and serum amyloid A in milk from dairy cows with chronic sub-clinical mastitis. Veterinary Research 36 191–198CrossRefGoogle ScholarPubMed
Hallén, E, Allmere, T, Näslund, J, Andrén, A & Lundén, A 2007 Effect of genetic polymorphism of milk proteins on rheology of chymosin-induced milk gels. International Dairy Journal 17 791–799CrossRefGoogle Scholar
Haryani, S, Datta, N, Elliott, AJ & Deeth, HC 2003 Production of proteinases by psychrotropic bacteria in raw milk stored at low temperature. Australian Journal of Dairy Technology 58 15–20Google Scholar
Hari-Dass, R, Shah, C, Meyer, DJ & Raynes, JG 2005 Serum amyloid A protein binds to outer membrane protein A of gram-negative bacteria. Journal of Biological Chemistry 280 18562–18567CrossRefGoogle ScholarPubMed
Hiss, S, Mielenz, M, Bruckmaier, RM & Sauerwein, H 2004 Haptoglobin concentrations in blood and milk after endotoxin challenge and quantification of mammary Hp mRNA expression. Journal of Dairy Science 87 3778–3784CrossRefGoogle ScholarPubMed
Hiss, S, Mueller, U, Neu-Zahren, A & Sauerwein, H 2007 Haptoglobin and lactate dehydrogenase measurements in milk for the identification of subclinically infected quarters. Veterinarni Medicina 52 245–252CrossRefGoogle Scholar
Horadagoda, NU, Knox, KMG, Gibbs, HA, Reid, SWJ, Horadagoda, A, Edwards, SER & Eckersall, PD 1999 Acute phase proteins in cattle: discrimination between acute and chronic inflammation. Veterinary Record 144 437–441CrossRefGoogle ScholarPubMed
Kelly, AL, O'Flaherty, FO & Fox, PF 2006 Indigenous proteolytic enzymes in milk: A brief overview of the present state of knowledge. International Dairy Journal 16 563–572CrossRefGoogle Scholar
Kitchen, BJ 1981 Review of the progress of dairy science: Bovine mastitis: milk compositional changes and related diagnostic tests. Journal of Dairy Research 48 167–188CrossRefGoogle ScholarPubMed
Larsen, LB, Rasmussen, MD, Bjerring, M & Nielsen, JH 2004 Proteases and protein degradation in milk from cows infected with Streptococcus uberis. International Dairy Journal 14 899–907CrossRefGoogle Scholar
Larson, MA, Weber, A, Weber, AT & McDonald, TL 2005 Differential expression and secretion of bovine serum amyloid A (SAA3) by mammary epithelial cells stimulated with prolactin or lipopolysaccahride. Veterinary Immunology and Immunopathology 107 255–264CrossRefGoogle ScholarPubMed
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 16 648–654CrossRefGoogle Scholar
Leitner, G, Silanikove, N, Jacobi, S, Weisblit, L, Bernstein, S & Merin, U 2008 The influence of storage on the farm and in dairy silos on milk quality for cheese production. International Dairy Journal 18 109–113CrossRefGoogle Scholar
Le Roux, Y, Colin, O & Laurent, F 1995 Proteolysis in samples of quarter milk with varying somatic cell counts: 1. Comparison of some indicators of endogenous proteolysis in milk. Journal of Dairy Science 78 1289–1297CrossRefGoogle ScholarPubMed
Lindmark-Månsson, H, Bränning, C, Aldén, G & Paulsson, M 2006 Relationship between somatic cell count, individual leukocyte populations and milk components in bovine udder quarter milk. International Dairy Journal 16 717–727CrossRefGoogle Scholar
Ma, Y, Ryan, C, Barbano, DM, Galton, DM, Rudan, MA & Boor, KJ 2000 Effects of somatic cell count on quality and shelf-life of pasteurized fluid milk. Journal of Dairy Science 83 264–274CrossRefGoogle ScholarPubMed
Mara, O, Roupie, C, Duffy, A & Kelly, AL 1998 The curd-forming properties of milk as affected by the action of plasmin. International Dairy Journal 8 807–812CrossRefGoogle Scholar
Mazal, G, Vianna, PCB, Santos, MV & Gigante, ML 2007 Effect of somatic cell count on prato cheese composition. Journal of Dairy Science 90 630–636CrossRefGoogle ScholarPubMed
McDonald, TL, Larson, MA, Mack, DR & Weber, A 2001 Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum. Veterinary Immunology and Immunopathology 83 203–211CrossRefGoogle ScholarPubMed
Munro, GL, Grieve, PA & Kitchen, BJ 1984 Effects of mastitis on milk yield, milk composition, processing properties and yield and quality of milk products. Australian Journal of Dairy Technology 39 7–16Google Scholar
Nielsen, BH, Jacobsen, S, Andersen, PH, Niewold, TA & Heegaard, PMH 2004 Acute phase protein concentrations in serum and milk from healthy cows, cows with clinical mastitis and cows with extramammary inflammatory conditions. Veterinary Record 154 361–365CrossRefGoogle ScholarPubMed
Saeman, AI, Verdi, RJ, Galton, DM & Barbano, DM 1988 Effect of mastitis on proteolytic activity in bovine milk. Journal of Dairy Science 71 505–512CrossRefGoogle ScholarPubMed
Santos, MV, Ma, Y & Barbano, DM 2003 Effect of somatic cell count on proteolysis and lipolysis in pasteurized fluid milk during shelf-life storage. Journal of Dairy Science 86 2491–2503CrossRefGoogle ScholarPubMed
Schaar, J 1985 Plasmin activity and proteose-peptone content of individual milks. Journal of Dairy Research 52 369–378CrossRefGoogle Scholar
Silanikove, N, Shamay, A, Shinder, D & Moran, A 2000 Stress down regulates milk yield in cows by plasmin induced β-casein product that blocks K+ channels on the apical membranes. Life Sciences 67 2201–2212CrossRefGoogle ScholarPubMed
Sørhaug, T & Stepaniak, L 1997 Psychrotrophs and their enzymes in milk and dairy products: Quality aspects. Trends in Food Science & Technology 18 35–41CrossRefGoogle Scholar
Urech, E, Puhan, Z & Schallibaum, M 1999 Changes in milk fraction as affected by subclinical mastitis. Journal of Dairy Science 82 2402–2411CrossRefGoogle ScholarPubMed
Wiking, L, Frost, MB, Larsen, LB & Qvist, KB 2002 Effects of storage conditions on lipolysis, proteolysis and sensory attributes in high quality raw milk. Milchwissenschaft 57 190–194Google Scholar