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Heat-induced changes in the secondary structure of hen egg S-ovalbumin

Solutions of hen egg S-ovalbumin at pD or pH 3.0, 1.0, and 9.0 were heated at temperatures between 30 and 90 o C to study changes in secondarg structure by Courier transform infrared spectroscopy (CTIR), storage moduli by dynamic rheological testing, and denaturation temperatures by differential scanning calorimetry. Second-derivative infrared spectra of native S-ovalbumin at pD 1.0 and 9.0 revealed protein absorption bands for Q-sheet (1626 cm -1 ), 3 10 -helix (1638 cm -1 ), α-helix (1656 cm -1 ) and turns (1682 and 1610 cm -1 )