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|Title:||Flexibility and viscometric studies of globular proteins ovalbumin and ovotransferrin|
|Authors:||Waris, B N|
Raziq, A H Abdul
|Abstract:||The ultrasonic velocity, density and viscosity of two egg proteins, ovalbumin and ovotransferrin in phosphate buffer have been studied at the physiological pH values. The thermodynamic functions for unfolding, ellipticity, surface amino acid residues and compressibility have been obtained for thermal and chemical denaturation in these food proteins. The com-puted values of Huggin’s constant and shape factor, at a fixed ionic strength 0.16 M are found to be in agreement with the reported values for globular proteins. The slow increase in free-energy of unfolding with temperature at a fixed pH 7 sug-gests uncoiling and in turn, disappearance of biological activity. It has been observed that the effects of temperature and chemical denaturant on the native protein may give rise to different conformational states. In the presence of urea and so-dium dodecyl sulphate (SDS), the proteins gave the excessively denatured states at 25ºC and pH 7, in comparison to the thermal denatured state. The positive values of partial adiabatic compressibility β<sub>s</sub> over the temperature range 45-75ºC suggest the possibility of large internal flexibility in ovotransferrin than in ovalbumin.|
|Appears in Collections:||IJBB Vol.40(2) [April 2003]|
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