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Inhibition of pancreatic and microbial lipases by proteins

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
0005-2760
Publisher
Elsevier
Publication Date
Volume
795
Issue
2
Identifiers
DOI: 10.1016/0005-2760(84)90082-1
Keywords
  • Lipase
  • Colipase
  • Protein Inhibition
  • Enzyme-Substrate Interface
  • (Pancreas
  • Rhizopus Spp)
Disciplines
  • Biology

Abstract

Abstract We have compared the effect of several proteins, including melittin, β-lactoglobulin A, serum albumin, ovalbumin and myoglobin, on the hydrolysis of tributyrin and triolein by upases from various origins. All proteins tested inactivate pancreatic lipase in absence of colipase and bile salt. Inhibition is not significantly reversed by colipase in absence of bile salt except in systems containing tributyrin and melittin or triolein and β-lactoglobulin A. In all other cases, activation of pancreatic lipase by colipase in presence of inhibitory protein requires the presence of bile salt. Lipase from Rhizopus delemar is also inhibited by the proteins that inactivate pancreatic lipase. In contrast, the activity of lipase from Rhizopus arrhizus is not affected by the proteins in the same concentration range. Inhibition of lipase activity by amphiphiles such as proteins or detergents appears to be a general phenomenon not directly related to a decrease in tension at the triacylglycerol-water interface. Inhibition could be the result of desorption of lipase from its substrate due to a change in interfacial quality.

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