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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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