Effect of high-pressure treatment at various temperatures on indigenous proteolytic enzymes and whey protein denaturation in bovine milk.
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 degrees 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 degrees 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 degrees C and at the pressures 450 and 650 MPa at 55 degrees C. Synergistic negative effects on the amount of native beta-lactoglobulin were observed at 450 and 650 MPa and on the amount of native alpha-lactalbumin at 650 MPa. There were significant correlations between enzymatic activities (PL, PA and cathepsin D) and the residual native beta-lactoglobulin and alpha-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.
Department of Food Science and Technology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece. mg@aua.gr
Golfo
G
Moatsou
Constantinos
C
Bakopanos
Dimitis
D
Katharios
George
G
Katsaros
Ioannis
I
Kandarakis
Petros
P
Taoukis
Ioannis
I
Politis
D000818:Animals; D002402:Cathepsin D / Q000378:metabolism; D005341:Fibrinolysin / Q000032:analysis; D007768:Lactalbumin / Q000378:metabolism; D007782:Lactoglobulins / Q000378:metabolism; D008892:Milk / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism*; D008894:Milk Proteins / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011312:Pressure; D011489:Protein Denaturation; D013696:Temperature; D000067816:Whey Proteins
D007782:Lactoglobulins; D008894:Milk Proteins; D000067816:Whey Proteins; D007768:Lactalbumin; D010447:Peptide Hydrolases; D005341:Fibrinolysin; D002402:Cathepsin D