ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1988.tb08982.x
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