Abstract
α-Lactalbumin and β-lactoglobulin solutions (in D 2 O) were heated at 50, 70, or 90 o C for 30, 60, or 90 min. Only the samples heated at 90 o C formed transparent gels. The amide I' and amide III' bands of the Raman spectra implicated an increase of β-sheet structure with a simultaneous decrease of helical structure in heard α-lactalbumin, while an increase of β-sheet with a simultaneous decrease of turn structure was suggested in heated β-lactoglobulin. Changes in other regions of the Raman spectra could be interpreted as changes in disulfide conformation as well as in microenmronment around several amino acid residues, i.e., Trp, Tyr, and His
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