JDS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Interpretive Summary
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Borda, D.
Right arrow Articles by Hendrickx, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Borda, D.
Right arrow Articles by Hendrickx, M.
J. Dairy Sci. 87:4042-4049
© American Dairy Science Association, 2004.

Mathematical Models for Combined High Pressure and Thermal Plasmin Inactivation Kinetics in Two Model Systems

D. Borda1, A. Van Loey2, C. Smout2 and M. Hendrickx2

1 Department of Food Bioengineering, Faculty of Food Science and Engineering, University Dunarea de Jos, 111 Domneasca Street, 800201 Galati, Romania
2 Laboratory of Food Technology, Department of Food and Microbial Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Heverlee, Belgium

Corresponding author: D. Borda; e-mail: daniela.borda{at}ugal.ro.

The combined high-pressure thermal inactivation kinetics of plasmin was studied in 2 model systems. The first system contained both plasmin and plasminogen, whereas, in the second system, all plasminogen was converted into plasmin, with urokinase, before the inactivation studies. High-pressure treatments were conducted in the range of 300 to 800 MPa combined with temperatures from 30 to 65°C. Under all conditions of pressure and temperature (isobaric-isothermal) studied, for both systems, first-order inactivation was observed. A third-degree polynomial model (derived from thermodynamic principles) successfully described the temperature and pressure dependence of the inactivation rate constant over the entire experimental domain. The antagonistic effect and the stabilization effect observed above a threshold pressure value of 600 MPa were thought to be related to the disruption of disulfide bonds in plasmin and plasminogen.

Key Words: plasmin • high pressure • kinetic • mathematical model

Abbreviation key: HP = high pressure






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by the American Dairy Science Association ®.