Online citations, reference lists, and bibliographies.
← Back to Search

The Kinetic Study Of Enzyme Action On Substrate Monolayers. Pancreatic Lipase Reactions.

J. W. Lagocki, J. Law, F. Kézdy
Published 1973 · Medicine, Chemistry

Save to my Library
Download PDF
Analyze on Scholarcy
Share
Abstract The enzymatic reaction of porcine pancreatic lipase with insoluble monolayers of either trioctanoin or 1,2-dioctanoin can be followed quantitatively by monitoring the considerable change in surface pressure which occurs during the course of the reaction. The rate of each reaction is proportional to the surface concentration of the substrate. The calculated pseudo-first order rate constants are proportional to the enzyme concentration in the bulk solution. At pH 7.6, the value of the second order rate constant for the hydrolysis of the primary ester function in trioctanoin was found to be 8.46 x 105 m-1 s-1, and that for dioctanoin, 2.65 x 104 m-1 s-1. The pH dependency of the rate constant for dioctanoin hydrolysis reveals an ionizable basic group at the active site of the enzyme with pKa of 6.38. The results are consistent with fully hydrated enzyme molecules acting upon substrate molecules lying within the insoluble mono-layer.
This paper references



This paper is referenced by
10.1021/BI00557A001
Properties of human apolipoprotein A-I at the air-water interface.
B. Shen (1980)
10.1016/j.colsurfb.2007.11.004
Action of Humicola lanuginosa lipase on mixed monomolecular films of tricaprylin and polyethylene glycol stearate.
T. Ivanova (2008)
10.1021/BI00626A011
Specificity of the phosphatidylcholine exchange protein from bovine liver.
H. H. Kamp (1977)
Methodological Aspects and Relevance of the Study of Vegetable Oil, Fat and Lipoprotein Oxidation Using Pancreatic Lipase and Arylesterase
M. Nus (2006)
HYDROLYSIS OF BUTTEROIL BY FIBER REACTOR: PART V. EFFECTS OF pH. IMMOBILIZED LIPASE USING A HOLLOW-
C. G. Hill (1993)
10.1016/0021-9797(76)90249-6
The surface pressure dependency of the enzymatic hydrolysis of lipid monolayers enzyme denaturation at the air-water interface
H. Cohen (1976)
10.1016/0003-9861(73)90540-7
Phospholipase A2 activity towards phosphatidylcholine in mixed micelles: surface dilution kinetics and the effect of thermotropic phase transitions.
E. Dennis (1973)
10.1007/BF01072932
A simple assay technique for pancreatic lipase
Robert E. Connon (2005)
10.1007/112_2015_24
The Secretion and Action of Brush Border Enzymes in the Mammalian Small Intestine.
D. Hooton (2015)
10.1002/BIT.260391003
Hydrolysis of butteroil by immobilized lipase using a hollow‐fiber reactor: Part II. Uniresponse kinetic studies
F. Malcata (1992)
In vitro effect of Triton WR-1339 on canine plasma high density lipoproteins.
K. Yamamoto (1984)
10.1016/0141-0229(92)90135-B
Kinetics and mechanisms of reactions catalysed by immobilized lipases.
F. Malcata (1992)
10.1111/J.1432-1033.1995.0892G.X
Kinetics of the two-step hydrolysis of triacylglycerol by pancreatic lipases.
A. Lykidis (1995)
10.1016/0009-3084(82)90052-4
Lipid-protein interactions in monolayers
R. Verger (1982)
10.1385/1-59259-581-2:279
Monolayer techniques for studying lipase kinetics.
S. Ransac (1999)
10.1016/S0162-0134(03)00177-6
Enzyme-catalysed siloxane bond formation.
A. Bassindale (2003)
10.1016/0300-9084(88)90188-5
Minireview on pancreatic lipase and colipase.
C. Chapus (1988)
10.1002/(SICI)1438-9312(200002)102:2<133::AID-EJLT133>3.0.CO;2-X
Methods for lipase detection and assay: a critical review
Frédéric Beisson (2000)
10.1016/S0076-6879(80)64016-6
[14] Enzyme kinetics of lipolysis
R. Verger (1980)
10.3109/10242429308997678
Hydrolysis of Butteroil by Immobilized Lipase Using a Hollow-Fiber Reactor: Part V. Effects of ph.
F. Malcata (1993)
10.1016/j.colsurfb.2011.03.018
Hydrolysis of mixed monomolecular films of tricaprylin/dilauroylphosphatidylcholine by lipase and phospholipase A₂.
K. Mircheva (2011)
10.7454/MST.V11I1.439
KINETIC MODEL FOR TRIGLYCERIDE HYDROLYSIS USING LIPASE: REVIEW
Heri Hermansyah (2009)
10.1016/S0167-4838(99)00047-3
Hydrolysis of emulsified mixtures of triacylglycerols by pancreatic lipase.
T. Käämbre (1999)
10.1016/S1381-1177(03)00052-3
Human digestive and metabolic lipases—a brief review
Manjari S. Mukherjee (2003)
10.1002/9780470122938.CH7
Pancreatic lipase and colipase: an example of heterogeneous biocatalysis.
M. Sémériva (1976)
10.1201/b10437-6
Enzymes and Thermally Oxidized Oils and Fats
Francisco S√°nchez-Muniz (2010)
10.1016/S0070-2161(08)60848-5
Enzymic Hydrolysis of Various Components in Biomembranes and Related Systems
M. Jain (1974)
10.1016/0927-7757(93)80119-Y
Lipase-catalyzed esterification in monolayers and microemulsions
C. Singh (1993)
A kinetic and molecular study of the lipase from Geobacillus thermoleovorans GE-7
Tobias George Barnard (2005)
Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces.
W. Momsen (1978)
10.1007/BF01870255
Phospholipases. III. Effects of ionic surfactants on the phospholipase-catalyzed hydrolysis of unsonicated egg lecithin liposomes
A. Goldhammer (2005)
10.1016/0001-8686(90)80023-S
Interactions of lipases with lipid monolayers. Facts and questions.
G. Piéroni (1990)
See more
Semantic Scholar Logo Some data provided by SemanticScholar