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Effect of Heat Treatment and Modification on Conformation and Flavor Binding by β‐Lactoglobulin
Author(s) -
O'NEILL T.,
KINSELLA J.E.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb08982.x
Subject(s) - chemistry , disulfide bond , flavor , conformational change , beta lactoglobulin , stereochemistry , biochemistry , whey protein
The flavor binding behavior of native β‐lactoglobuIin (β‐Lg) was significantly altered by thermal or chemical modification. Upon heat‐treatment at 75°C for 10 and 20 minutes the binding affinity for 2‐nonanone was reduced and the number of sites for binding was increased. This was related to conformational changes and aggregation of β‐Lg. Reduction of the disulfide bonds and ethylation of carboxylic acid groups also induced conformational changes which reduced the binding affinity of β‐Lg for 2‐nonanone.