Chee, C and Owusu-Apenten, Richard (2004) Sulfhydryl group activation for commercial beta-lactoglobulin measured using kappa-casein 2-thio, 5 ' nitrobenzoic acid. International Dairy Journal, 14 (3). pp. 195-200. [Journal article]
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The process of activation converts protein sulfhydryl (SH) groups from the masked state to a free state with increased reactivity. Beta-lactoglobulin (beta-Lg) SH group activation was measured, in phosphate buffer (pH 6.8) using K-casein 2-thio, 5'-nitrobenzoic acid (Cn-Ellman), at 412 nm. Reaction transition state parameters from 25-55degreesC and 60-80degreesC were not significantly different. Present results were compared with differential scanning calorimetry (DSC) traces for beta-Lg heat unfolding, temperature-reaction profiles for whey or beta-Lg heat aggregation, and also SH-activation in skim milk. The findings reveal that SH-group activation precedes heat unfolding and aggregation of beta-Lg. Further studies using protein disulfide reagents such. as Cn-Ellman will help to elucidate the mechanism of SH group activation for beta-Lg.
|Item Type:||Journal article|
|Keywords:||beta-Lactoglobulin; sulfhydryl activation; heat aggregation; kappa-casein, milk protein|
|Faculties and Schools:||Faculty of Life and Health Sciences|
Faculty of Life and Health Sciences > School of Biomedical Sciences
|Research Institutes and Groups:||Biomedical Sciences Research Institute|
Biomedical Sciences Research Institute > Northern Ireland Centre for Food and Health (NICHE)
|Deposited By:||Dr Richard Owusu-Apenten|
|Deposited On:||17 Aug 2010 11:27|
|Last Modified:||28 Jan 2014 14:46|
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