Study of the interaction of pancreatic lipase with procyanidins by optical and enzymatic methods.
Journal of agricultural and food chemistry, ISSN: 1520-5118, Vol: 58, Issue: 22, Page: 11901-11906
2010
- 58Citations
- 53Captures
- 1Mentions
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Metrics Details
- Citations58
- Citation Indexes58
- 58
- CrossRef47
- Captures53
- Readers53
- 53
- Mentions1
- News Mentions1
- News1
Most Recent News
Effects of Grape Seed Proanthocyanidin Extract on Obesity
ABSTRACT Obesity is a chronic metabolic disease resulting from excessive fat accumulation and/or abnormal distribution caused by multiple factors. As a major component of metabolic
Article Description
The interactions between porcine pancreatic lipase (PL) and grape seed procyanidins were studied by an enzymatic assay, fluorescence quenching, nephelometry, and dynamic light scattering (DLS). An inhibitory effect of grape seed procyanidins on lipase hydrolytic activity was found. Both the inhibition of lipase activity by procyanidins and the respective quenching of intrinsic protein fluorescence increased with the average degree of polymerization of the tested procyanidins. The association between procyanidins and enzyme involves a specific interaction as inferred from the fluorescence assays despite not changing significantly the tertiary structure of the protein. For all tested procyanidins it was shown, both by DLS and by nephelometry, that an increase in aggregation occurs up to a stoichiometric maximum after which further procyanidin addition causes a decrease in aggregation of aggregates. The maximum size of aggregates was shown to be closely related to the maximum overall aggregation. It was also shown that the inhibition of enzyme activity is to a large extent independent of the formation of aggregates.
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