Peptic proteolysis of esterified beta-casein and beta-lactoglobulin.
Moderate esterification induces slight secondary structure changes in two major milk proteins, beta-lactoglobulin and beta-casein. Esterification of beta-lactoglobulin prompts its tertiary structure 'melting', opening it to peptic cleavage. Twenty-two new cleavage sites were characterised in beta-lactoglobulin and five in beta-casein. Some of them are due to esterification-improved peptide bond accessibility, some to the bias of pepsin specificity by glutamate and aspartate esters. The resulting fragmentation yields original and partially amphiphilic peptide populations.
Briand
L
L
National Institute for Argronomic Research, Laboratory for the Study of Interactions of Food Molecules, Nantes, France.
Chobert
J M
JM
Haertlé
T
T
D000595:Amino Acid Sequence; D000818:Animals; D002364:Caseins / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004951:Esterification; D004952:Esters; D006868:Hydrolysis; D007782:Lactoglobulins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D010434:Pepsin A / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding
D002364:Caseins; D004952:Esters; D007782:Lactoglobulins; D010446:Peptide Fragments; D010434:Pepsin A