Secondary structure changes and peptic hydrolysis of beta-lactoglobulin induced by diols.
The addition of ethylene glycol, and 1,2- and 1,3-propanediol, decreases the bulk dielectric constant of the medium, and according to CD measurements, increases significantly the proportion of helical structure in beta-lactoglobulin. The medium-induced folding changes followed by limited peptic hydrolysis show that the cleavage of beta-lactoglobulin by pepsin is triggered by structural transformations induced by ethylene glycol only and not by 1, 2- and 1, 3-propanediol. Density measurements, at constant chemical potential and constant molality, demonstrate that all diols are present in the immediate domain of the protein. They are engaged in hydrophobic interactions with the amino acids of beta-lactoglobulin core inducing the formation of additional alpha-helices.
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Institut National de la Recherche Agronomique Laboratoire d'Etude des Interactions des Molécules Alimentaires, Nantes, France.
Chobert
J M
JM
Dalgalarrondo
M
M
Haertlé
T
T
D000438:Alcohols / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D019855:Ethylene Glycol; D005026:Ethylene Glycols / Q000494:pharmacology*; D005947:Glucose / Q000494:pharmacology; D006868:Hydrolysis; D007782:Lactoglobulins / Q000737:chemistry* / Q000378:metabolism*; D010434:Pepsin A / Q000378:metabolism*; D019946:Propylene Glycol; D011409:Propylene Glycols / Q000494:pharmacology*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013395:Sucrose / Q000494:pharmacology
D000438:Alcohols; D005026:Ethylene Glycols; D007782:Lactoglobulins; D011409:Propylene Glycols; D013395:Sucrose; C041787:1,3-propanediol; D019946:Propylene Glycol; D010434:Pepsin A; D019855:Ethylene Glycol; D005947:Glucose