Adsorbed protein secondary and tertiary structures by circular dichroism and infrared spectroscopy with refractive index matched emulsions.
The secondary structure of protein adsorbed at the emulsion interface has been studied in refractive index matched emulsions using the techniques of circular dichroism (CD) and Fourier transform infrared spectroscopy. Bovine serum albumin (BSA) and bovine beta-lactoglobulin (betalg) stabilized emulsions were studied, and the refractive index was altered by the addition of glycerol or polyethylene glycol. The effect of additive on the solution and adsorbed protein structure in addition to the effect of adsorption time was considered. Both adsorption and glycerol addition alter protein secondary structure; however, the majority of secondary structure remains. Small changes are observed in the secondary structure of adsorbed protein with time. Near-ultraviolet CD studies showed the effect of glycerol and adsorption on the aromatic groups. BSA showed small changes both upon the addition of glycerol to protein in solution and upon adsorption. betalg showed slightly larger changes upon the addition of glycerol to protein in solution and a larger change upon adsorption.
Husband
F A
FA
Institute of Food Research, Norwich Research Park, Colney Lane, Norwich NR4 7UA, United Kingdom.
Garrood
M J
MJ
Mackie
A R
AR
Burnett
G R
GR
Wilde
P J
PJ
D000327:Adsorption; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004655:Emulsions; D007768:Lactalbumin / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000379:methods
D004655:Emulsions; D012710:Serum Albumin, Bovine; D007768:Lactalbumin