Effect of Heat Treatment and Modification on Conformation and Flavor Binding by β‐Lactoglobulin

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.