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Effect of high-pressure treatment at various temperatures on indigenous proteolytic enzymes and whey protein denaturation in bovine milk

Published online by Cambridge University Press:  02 June 2008

Golfo Moatsou ,
Constantinos Bakopanos ,
Dimitis Katharios ,
George Katsaros ,
Ioannis Kandarakis ,
Petros Taoukis  and
Ioannis Politis
Golfo Moatsou*
Affiliation:
Department of Food Science and Technology, Agricultural University of Athens, Iera Odos 75, 11855, Athens, Greece
Constantinos Bakopanos
Affiliation:
Department of Food Science and Technology, Agricultural University of Athens, Iera Odos 75, 11855, Athens, Greece
Dimitis Katharios
Affiliation:
Vivartia S.A., 16, Irinis Avenue, 17778, Athens, Greece
George Katsaros
Affiliation:
School of Chemical Engineering, National Technical University of Athens, Chemical Engineering Building, Zographou Campus, Athens, Greece
Ioannis Kandarakis
Affiliation:
Department of Food Science and Technology, Agricultural University of Athens, Iera Odos 75, 11855, Athens, Greece
Petros Taoukis
Affiliation:
School of Chemical Engineering, National Technical University of Athens, Chemical Engineering Building, Zographou Campus, Athens, Greece
Ioannis Politis
Affiliation:
Department of Animal Science, Agricultural University of Athens, Iera Odos 75, 11855, Athens, Greece
*
*For correspondence; e-mail: mg@aua.gr
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Abstract

The objective of the present study was to determine the effect of high pressure (HP) processing (200, 450 and 650 MPa) at various temperatures (20, 40 and 55°C) on the total plasmin plus plasminogen-derived activity (PL), plasminogen activator(s) (PA) and cathepsin D activities and on denaturation of major whey proteins in bovine milk. Data indicated that transfer of both PL and PA from the casein micelles to milk serum occurred at all pressures utilized at room temperature (20°C). In addition to the transfer of PL and PA from micelles, there were reductions in activities of PL (16–18%) and PA (38–62%) for the pressures 450 and 650 MPa, at room temperature. There were synergistic negative effects between pressure and temperature on residual PL activity at 450 and 650 MPa and on residual PA activity only at 450 MPa. Cathepsin D activity in the acid whey from HP-treated milk was in general baroresistant at room temperature. The residual activity of cathepsin D decreased significantly at 650 MPa and 40°C and at the pressures 450 and 650 MPa at 55°C. Synergistic negative effects on the amount of native β-lactoglobulin were observed at 450 and 650 MPa and on the amount of native α-lactalbumin at 650 MPa. There were significant correlations between enzymatic activities (PL, PA and cathepsin D) and the residual native β-lactoglobulin and α-lactalbumin in bovine milk. In conclusion, HP significantly affected the activity of indigenous proteolytic enzymes and whey protein denaturation in bovine milk. Reduction in activity of indigenous enzymes (PL, PA and cathepsin D) and transfer of PL and PA from the casein to milk serum induced by HP is expected to have a profound effect on cheese yield, proteolysis during cheese ripening and quality of UHT milk during storage.

Keywords

High pressureplasminplasminogen activatorscathepsin Dwhey proteins
Type
Research Article
Information
Journal of Dairy Research , Volume 75 , Issue 3 , August 2008 , pp. 262 - 269
Copyright
Copyright © Proprietors of Journal of Dairy Research 2008

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References

Bastian, ED & Brown, RJ 1996 Plasmin in milk and dairy products: An update. International Dairy Journal 6 435–437CrossRefGoogle Scholar
Borda, D, Indrawati, , Smout, C, Van Loey, A & Hendrickx, M 2004 High pressure thermal inactivation of a plasmin system. Journal of Dairy Science 87 2351–2358CrossRefGoogle ScholarPubMed
Considine, T, Patel, HA, Anema, SG, Singh, H & Creamer, LK 2007 Interactions of milk proteins during heat and high hydrostatic pressure treatment-A review. Innovative Food Science and Emerging Technologies 8 1–23CrossRefGoogle Scholar
García-Risco, MR, Cortes, E, Carrascosa, AV & López-Fandiňo, R 2003 Plasmin activity in pressurized milk. Journal of Dairy Science 86 728–734CrossRefGoogle ScholarPubMed
García-Risco, MR, Olano, A, Ramos, M & López-Fandiňo, R 2000 Micellar changes induced by high pressure. Influence in the proteolytic activity and organoleptic properties of milk. Journal of Dairy Science 83 2184–2189CrossRefGoogle Scholar
Gaucheron, F, Famelart, MH, Marieyye, F, Raulot, K, Michel, F & LeGraet, Y 1997 Combined effects of temperature and high-pressure treatments on physicochemical characteristics of skim milk. Food Chemistry 59 439–447CrossRefGoogle Scholar
Hayes, MG, Hurley, MJ, Larsen, LB, Heegaard, CW, Magboul, AAA, Oliveira, JC, McSweeney, PLH, & Kelly, AL 2001 Thermal inactivation kinetics of bovine cathepsin D. Journal of Dairy Research 68 267–276CrossRefGoogle ScholarPubMed
Hinrichs, J & Rademacher, B 2005 Kinetics of combined thermal and pressure-induced whey proteins deanturation in bovine skim milk. International Dairy Journal 15 315–323CrossRefGoogle Scholar
Huppertz, T, Fox, PF & Kelly, AL 2004a High pressure-induced denaturation of α-lactalbumin and β-lactoglobulin in bovine milk and whey: a possible mechanism. Journal of Dairy Research 71 489–495CrossRefGoogle ScholarPubMed
Huppertz, T, Fox, PF & Kelly, AL 2004b High-pressure treatment of bovine milk: effects on casein micelles and whey proteins. Journal of Dairy Research 71 97–106CrossRefGoogle ScholarPubMed
Huppertz, T, Fox, PF & Kelly, AL 2004c Plasmin activity and proteolysis ih high-pressure treated milk. Le Lait 84 297–304CrossRefGoogle Scholar
Huppertz, T, Smiddy, MA, Upadhyay, VK & Kelly, AL 2006 High-pressure-induced changes in bovine milk: a review. International Journal of Dairy Technology 59 58–66CrossRefGoogle Scholar
Hurley, MJ, Larsen, LB, Kelly, AL & McSweeney, PLH 2000a Cathepsin D activity in quarg. International Dairy Journal 10 453–458CrossRefGoogle Scholar
Hurley, MJ, Larsen, LB, Kelly, AL & McSweeney, PLH 2000b The milk acid proteinase cathepsin D: a review. International Dairy Journal 10 673–681CrossRefGoogle Scholar
Ismail, B, Choi, LH, Were, LM & Nielsen, SS 2006 Activity and nature of plasminogen activators associated with the casein micelle. Journal of Dairy Science 89 3285–3295CrossRefGoogle ScholarPubMed
Kelly, AL, O'Flaherty, F & Fox, PF 2006 Indigenous proteolytic enzymes in milk: A brief overview of the present stage of knowledge. International Dairy Journal 16 563–572CrossRefGoogle Scholar
Larsen, LB, McSweeney, PLH, Hayes, MG, Andersen, JB, Ingvartsen, KL & Kelly, AL 2006 Variation in activity and heterogeneity of bovine milk proteases with stage of lactation and somatic cell count. International Dairy Journal 16 1–8CrossRefGoogle Scholar
Larsen, LB, Wium, H, Benfeldt, C, Heegaard, CW, Ardo, Y, Qvist, KB & Petersen, TE 2000 Bovine milk procathepsin D: presence and activity in heated milk and in extracts of rennet-free UF-Feta cheese. International Dairy Journal 10 67–73CrossRefGoogle Scholar
Larsen, LB, Benfeldt, C, Rasmussen, LK & Petersen, TE 1996 Bovine milk procathepsin D and cathepsin D: Coagulation and milk protein degradation. Journal of Dairy Research 63 119–130CrossRefGoogle ScholarPubMed
López-Fandiňo, R 2006 High pressure-induced changes in milk proteins and possible applications in dairy technology. International Dairy Journal 16 1119–1131CrossRefGoogle Scholar
López-Fandiňo, R, Carrascosa, AV & Olano, A 1996 The effects of high pressue denaturation and cheese-making properties of raw milk. Journal of Dairy Science 79 929–936CrossRefGoogle Scholar
Magboul, AAA, Larsen, LB, McSweeney, PLH & Kelly, AL 2001 Cysteine protease activity in bovine milk. International Dairy Journal 11 865–872CrossRefGoogle Scholar
Moatsou, G, Hatzinaki, A, Kandarakis, I & Anifantakis, E 2003 Nitrogenous fractions during the manufacture of whey protein concentrates from Feta cheese whey. Food Chemistry 81 209–217CrossRefGoogle Scholar
Needs, EC, Stenning, RA, Gill, AL, Ferragut, V & Rich, GT 2000 High-pressure treatment of milk: effects on casein micelle structure and on enzymatic coagulation. Journal of Dairy Research 67 31–42CrossRefGoogle Scholar
Ο'Driscoll, BM, Rattray, FP, McSweeney, PLH & Kelly, AL 1999 Protease activities in raw milk determined using a synthetic heptapeptide substrate. Journal of Food Science 64 606–611CrossRefGoogle Scholar
O'Reilly, CE, Kelly, AL, Murphy, PM & Beresford, TP 2001 High pressure treatment: Applications in cheese manufacture and ripening. Trends in Food Science and Technology 12 51–59CrossRefGoogle Scholar
Politis, I, Zavizion, B, Barbano, DM & Gorewit, RC 1993 Enzymatic assay for the combined determination of plasmin plus plasminogen in milk: Revisited. Journal of Dairy Science 76 1260–1267CrossRefGoogle Scholar
Scollard, PG, Beresford, TP, Murphy, PM & Kelly, AL 2000a Barostability of milk plasmin activity. Le Lait 80 609–619CrossRefGoogle Scholar
Scollard, PG, Beresford, TP, Needs, EC, Murphy, PM & Kelly, AL 2000b Plasmin activity, β-lactoglobulin denaturation in high-pressure-treated milk. International Dairy Journal 10 835–841CrossRefGoogle Scholar
White, JH, Zavision, B, O'Hare, K, Gilmore, J, Guo, MR, Kindstedt, P & Politis, I 1995 Distribution of plasminogen activators in different fractions of bovine milk. Journal of Dairy Research 62 115–122CrossRefGoogle ScholarPubMed