Study of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometry

Meat batter proteins—Effect of chemical modification on structure

“…Cheung (1969) found a reduction in the fluorescence of myosin in the presence of urea using a probe method. Ma and Harwalkar (1988) also reported similar observations with oat globulin. However, they observed a significant red shift in the emission maxima which was not found here (Fig 2, line iv).…”

“…Hence, the results for the H,O,-treated batter suggest a greater quenching of the Trp fluorescence. This may be because of the increased efficiency of the non-radiative mechanisms due to the greater number of disulphide bonds which were present in the proteins (Penzer 1980; Ma and Harwalkar 1988).…”

Altering functional attributes of proteins through cross linking by transglutaminase – A case study with whey and seed proteins

“…Similar increase in the thermal stability of oat globulin has been attributed to the formation of aggregates with compact network (Ma & Harwalkar, 1988;Nai, Ching, Wai, & Yoshinori, 2002). Effects of heat treatment on proteins are important since heat often diminishes solubility (Kinsella, 1976).…”

Interaction of biocompatible sugar based surfactant n-dodecyl β-d-maltoside with lysozyme

“…3(a) and (b), respectively. The fluorescence intensity at both excitation wavelengths increases on the gradual addition of C 12 G 2 and the λ max slightly shifted towards the shorter wavelength (blue shift), characteristic of unfolding of the protein [41]. The rise in the fluorescence intensity indicated that the fluorophores are more exposed to the light, in addition, the blue shift is either due to the nonpolar interaction between hydrophobic moiety of surfactant and exposed fluorophores (possible with unfolding which is likely to happen, in our case, as there are less chances of the polar interactions between the lysozyme with C 12 G 2 owing to nonionic nature of the latter) or movement of fluorophores towards interior hydrophobic core of the protein, which is probable when proteins fold [33].…”