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Flexibility and viscometric studies of globular proteins ovalbumin and ovotransferrin

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Title Flexibility and viscometric studies of globular proteins ovalbumin and ovotransferrin
 
Creator Waris, B N
Bano, B
Raziq, A H Abdul
 
Description 98-107
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 βs over the temperature range 45-75ºC suggest the possibility of large internal flexibility in ovotransferrin than in ovalbumin.
 
Date 2009-04-06T10:23:12Z
2009-04-06T10:23:12Z
2003-04
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3746
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol.40(2) [April 2003]