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


     

Journal of Dairy Science Vol. 79 No. 1 27-32
© 1996 by American Dairy Science Association ®
This Article
Right arrow Full Text (PDF)
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 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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Barton, R. H.
Right arrow Articles by Turner, K. W.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Barton, R. H.
Right arrow Articles by Turner, K. W.

Characteristics of Tributyroylglycerol Hydrolysis Mediated by Partially Purified Lamb Pregastric Lipase

Richard H. Barton 1, Charmian J. O'connor 1, and Keith W. Turner 2

1 Department of Chemistry, The University of Auckland PB 92019, Auckland, New Zealand
2 New Zealand Rennet Company Ltd., PO Box 122, Eltham, New Zealand

A partially purified pregastric lipase from lambs was used as a catalyst for the hydrolysis of tributyroylglycerol. The reaction was followed by pH-stat autotitration of the released butyric acid. Integral values for pH and temperature were selected for determination of full Michaelis-Menten plots, and a kinetic surface was derived to characterize the activity of the enzyme preparation over a wide combination of these conditions. This surface enclosed a region of maximum activity centered on optimal pH (pH 6.4) and temperature (43°C), although optima were not sharply delineated. The activity in the surrounding region was generally high, and the value of the Michaelis-Menten constant was < 0.2 mM, indicating that tributyroylglycerol was generally a highly favored substrate.

Key Words: lamb • pregastric lipase • hydrolysis • tributyroylglycerol

Submitted on April 10, 1995
Accepted on September 5, 1995




This article has been cited by other articles:


Home page
 J DAIRY SCIHome page
M. V. Calvo and J. Fontecha
Purification and Characterization of a Pregastric Esterase From a Hygienized Kid Rennet Paste
J Dairy Sci, May 1, 2004; 87(5): 1132 - 1142.
[Abstract] [Full Text] [PDF]

Home page
 Journal of Bioactive and Compatible PolymersHome page
C. J. O'Connor and R. D. Manuel
Calf Pregastric Lipase Catalyzed Hydrolysis of 4-Nitrophenylalkanoates and Anhydrous Milk Fat: Effect of pH, Temperature and Acyl Carbon Chain Length
Journal of Bioactive and Compatible Polymers, September 1, 2000; 15(5): 406 - 424.
[Abstract] [PDF]

Home page
 Journal of Bioactive and Compatible PolymersHome page
C. J. O'Connor, D. T. Lai, and R. H. Barton
Lamb Pregastric Lipase Activity: Catalyzed Hydrolysis of Dibutyryl-1,2(3)-Propanediols and Butyryl-1(2)-Propanol and Inhibition of the Catalyzed Hydrolysis of Tributyrylglycerol in the Presence of EDTA, LiCl, NaCl and Ethanol
Journal of Bioactive and Compatible Polymers, April 1, 1998; 13(2): 124 - 135.
[Abstract]

Home page
 Journal of Bioactive and Compatible PolymersHome page
C. J. O'Connor, D. T. Lai, and C. Q. Sun
Calf Pregastric Esterase Catalyzed Hydrolysis of 4-Nitrophenylalkanoates: pH and Temperature Effects
Journal of Bioactive and Compatible Polymers, April 1, 1997; 12(2): 140 - 154.
[Abstract]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by the American Dairy Science Association ®.