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In vitro inhibition of lipase activity by malonaldehyde, formaldehyde and propionaldehyde
Author(s) -
Landsberg J. D.,
Sinnhuber R. O.
Publication year - 1965
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02541166
Subject(s) - propionaldehyde , lipase , chemistry , formaldehyde , in vitro , methanol , chromatography , biochemistry , organic chemistry , enzyme , aldehyde , catalysis
The in vitro inhibition of bovine pancreatic lipase by malonaldehyde, formaldehyde and propionaldehyde was investigated. Malonaldehyde, as sodium 3‐oxy‐prop‐2‐enal (MA‐Na), was found to be the most inhibitory at pH values below 7. Its reaction with lipase appeared to be two part: the first was rapid and a function of the MA‐Na concentration; the second part was slower and related linearly to the MA‐Na concentration. Methanol‐free formaldehyde was a much less effective inhibitor. Low concentrations (0.01 M) had little effect on lipse activity. Propionaldehyde produced the least inhibition. A break point in the reaction of propionaldehyde with lipase occurred with time. After the break point, the inhibition nearly parallelled that seen in the control.