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Abstract
Aggregation of beta-lactoglobulin occurs mainly via intermolecular disulphide bond exchange. Upon heating, beta-lactoglobulin aggregated which increased with increasing pH. The presence of DTT led to more rapid aggregation and precipitation of beta-lactoglobulin. Alpha-Crystallin prevented the aggregation of heat-stressed beta-lactoglobulin and was a more efficient chaperone at higher pH values. In the presence of DTT, however, alpha-crystallin was a less efficient chaperone due to faster aggregation of heated and reduced beta-lactoglobulin.
Highlights
Beta-lactoglobulin is a major whey protein of milk[1,2,3], which at physiological pH values exists as a dimer[4,5]
At pH values of 7.5, 7.0 and 6.5 at the same time point, alpha-crystallin prevented the aggregation of beta-lactoglobulin by approximately 34, 15 and 14% respectively. These results show that DTT increased the rate of aggregation of heated betalactoglobulin and in this situation alpha-crystallin is a less efficient chaperone in preventing the aggregation of beta-lactoglobulin
Beta-lactoglobulin aggregates via a combination of disulphide bond exchange and a nucleation-dependent mechanism due to hydrophobic association[26,27]
Summary
Beta-lactoglobulin is a major whey protein of milk[1,2,3], which at physiological pH values exists as a dimer[4,5]. Betalactoglobulin dissociates into monomers, leading to exposure of hydrophobic groups and the free sulfhydryl group[9,10]. This gives rise to aggregation and/or polymerization[4,5,9,11,12]. Beta-lactoglobulin is sensitive to heating at 60-100°C. The protein undergoes an initial dissociation of dimers followed by conformational changes which increase the exposure of previously buried hydrophobic groups and the thiol group[4,9,12,13,14]
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