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Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin

Published online by Cambridge University Press:  01 June 2009

Henrik Stapelfeldt ,
Per Hjort Petersen ,
Kristian Rotvig Kristiansen ,
Karsten Bruun Qvist  and
Leif H. Skibsted
Henrik Stapelfeldt
Affiliation:
Department of Dairy and Food Science, Royal Veterinary and Agricultural University, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark
Per Hjort Petersen
Affiliation:
Institute for Dairy Research, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark
Kristian Rotvig Kristiansen
Affiliation:
Institute for Dairy Research, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark
Karsten Bruun Qvist
Affiliation:
Institute for Dairy Research, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark
Leif H. Skibsted
Affiliation:
Department of Dairy and Food Science, Royal Veterinary and Agricultural University, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark
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Summary

Hydrolysis of β-lactoglobulin B (β-lg B) by pepsin, a process slow at ambient conditions, is facilitated at a moderately high hydrostatic pressure such as 300 MPa, corresponding to an apparent volume of activation ΔV# = −63 ml mol−1 at pH 2·5, 30 °C and Γ/2=0·16. Digestion of β-lg by trypsin and thermolysin is likewise enhanced by pressure, and the pressure effect has been traced to pressure denaturation of β-lg B, which by high-pressure fluorescence spectroscopy has been shown to have a large negative volume of reaction, ΔV° = −98 ml mol−1, at pH 6·7, 30 °C and Γ/2 = 0·16. Pressure denaturation is only slowly reversed following release of pressure and the enhanced digestibility is maintained at ambient pressure for several hours.

Type
Original Articles
Information
Journal of Dairy Research , Volume 63 , Issue 1 , February 1996 , pp. 111 - 118
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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