Journal
PROCESS BIOCHEMISTRY
Volume 49, Issue 2, Pages 237-243Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2013.10.018
Keywords
Pancreatic lipase (PL); Proanthocyanidins (PC); Conformation; Thermodynamics; Kinetics
Categories
Funding
- Natural Science Foundation of China [31270858, 31070709]
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The interactions between proanthocyanidins (PC) and porcine pancreatic lipase (PL) were investigated from variant aspects of lipase conformation, activity, kinetics, and thermodynamics. Results show that 34% inhibitory rate of PC on PL is achieved after about 30-min incubation, and the inhibitory rate increases with the increase of PC concentration and then plateaus at the PC/PL ratio of 200. Circular dichroism and fluorescence spectroscopic analyses demonstrate that PC decreases the alpha-helix content while increases the beta-sheet content of PL, but does not change the microenvironment of Trp, and PC quenches the fluorescence of PL both dynamically and statically through the formation of PL-PC complex. PC induces PL aggregation and then stabilizes the lipase aggregates. Kinetic studies reveal that PC does not change the K-m value while decreases the V-max value, implying that PC non-competitively inhibits the PL activity. (c) 2013 Elsevier Ltd. All rights reserved.
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