scholarly journals The adsorption to and hydrolysis of 1,3-didecanoyl glycerol monolayers by pancreatic lipase. Effects of substrate packing density.

1981 ◽  
Vol 256 (13) ◽  
pp. 6913-6916
Author(s):  
W.E. Momsen ◽  
H.L. Brockman
Keyword(s):  
Pancreatic Lipase ◽  
Packing Density ◽  
Hydrolysis Of

Hydrolysis of intralipid by pancreatic lipase and phospholipase A2-gel filtration studies

Lipids ◽  
1985 ◽  
Vol 20 (11) ◽  
pp. 765-772 ◽  
Author(s):  
Renée Grataroli ◽  
Monique Charbonnier ◽  
Gilles Nalbone ◽  
Denis Lairon ◽  
Christiane Chabert ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Pancreatic Lipase ◽  
Gel Filtration ◽  
Hydrolysis Of

Hydrolysis of emulsified mixtures of triacylglycerols by pancreatic lipase

1999 ◽  
Vol 1431 (1) ◽  
pp. 97-106 ◽  
Author(s):  
Tuuli Käämbre ◽  
Vello Tõugu ◽  
Peeter Käämbre ◽  
Heiki Vija ◽  
Peeter Sikk
Keyword(s):  
Pancreatic Lipase ◽  
Hydrolysis Of

MECHANISM OF ACTIVATION OF HOG PANCREATIC LIPASE BY SODIUM TAUROCHOLATE

1963 ◽  
Vol 41 (1) ◽  
pp. 719-730 ◽  
Author(s):  
Paul J. Fritz ◽  
Paul Melius
Keyword(s):  
Activation Energy ◽  
Enzymatic Hydrolysis ◽  
Pancreatic Lipase ◽  
Sodium Taurocholate ◽  
Enzyme Complex ◽  
Temperature Dependent ◽  
Fast Reaction ◽  
Presence And Absence ◽  
Hydrolysis Of

A new preparation of hog pancreatic lipase is described which is evidently the most stable one of its kind. From the composition of the reaction mixtures after enzymatic hydrolysis with and without sodium taurocholate, it appears that the hydrolysis of triglyceride to diglyceride is facilitated and the hydrolysis of diglyceride to monoglyceride is depressed in the presence of taurocholate. The differences in the curves showing the rates of hydrolysis of triolein, monoolein, tributyrin, and monobutyrin in the presence and absence of taurocholate also indicate that the taurocholate acts to split the diglyceride–enzyme complex and thus increases the action of the enzyme on the triglyceride ester. The hydrolysis of the triglyceride is a fast reaction whereas the di- and mono-glycerides are hydrolyzed at much slower rates. The activation energy for the lipolysis of the triolein and tributyrin has been calculated in the presence and absence of taurocholate. This was possible because in spite of earlier reports that the lipolysis of triolein was not temperature dependent between 10 and 40 degrees, we found these reactions to be temperature dependent. The lesser activating effect at the highest taurocholate concentrations indicates this is not a simple emulsifying effect.

Selective Acetate Hydrolysis of Diastereomers with Porcine Pancreatic lipase (PPL) as an Access to Useful Chiral Building Blocks

1992 ◽  
Vol 1992 (11) ◽  
pp. 1131-1135 ◽  
Author(s):  
Johann Mulzer ◽  
Stefan Greifenberg ◽  
Anne Beckstett ◽  
Matthias Gottwald
Keyword(s):  
Pancreatic Lipase ◽  
Building Blocks ◽  
Porcine Pancreatic Lipase ◽  
Hydrolysis Of

Enzymes in organic synthesis. 36. Synthesis of optically active civet constituent from an enzyme-generated chiral synthon

1987 ◽  
Vol 65 (4) ◽  
pp. 704-707 ◽  
Author(s):  
J. Bryan Jones ◽  
R. Scott Hinks
Keyword(s):  
Acetic Acid ◽  
Organic Synthesis ◽  
Pancreatic Lipase ◽  
Optically Active ◽  
Starting Material ◽  
Porcine Pancreatic Lipase ◽  
Hydrolysis Of ◽  
Enzymes In Organic Synthesis ◽  
Chiral Synthon

A synthesis of the civet constituent, (+)-(S,S)-(cis-6-methyltetrahydropyran-2-yl)acetic acid, is described, in which the key stereochemistry of the chiral starting material is set by an enantiotopically selective, porcine pancreatic lipase-catalyzed, hydrolysis of a meso diester.

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