Identification of amino acids in human colipase that mediate adsorption to lipid emulsions and mixed micelles.

ABSTRACT: The adsorption of colipase is essential for pancreatic triglyceride lipase activity and efficient dietary fat digestion. Yet, little is known about which specific amino acids in the hydrophobic surface of colipase influence adsorption. In this study, we systematically substituted alanine or tryptophan at residues implicated in adsorption of colipase to an interface. We expressed, purified recombinant colipase mutants and characterized the ability of each alanine mutant to restore activity to lipase in the presence of bile salts. The functions of L16A, Y55A, I79A and F84A colipase were most impaired with activities ranging from 20 to 60% of wild-type colipase. We next characterized the fluorescence properties of the tryptophan mutants in the absence and presence of bile-salt-oleic acid mixe

SUBMITTER: Ross LE 

PROVIDER: S-EPMC3642234 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature