Correlation of the Protein Structure and Gelling Properties in Dried Egg White Products

Abstract

The relationship between protein structure and aggregation, as well as heat-induced gelling properties, of seven dried egg white (DEW) products was investigated. Strong correlations were found between average molecular weight and hydrophobicity plus surface SH groups of DEW-soluble protein aggregate (SPA). This suggests that hydrophobic interactions and disulfide bond formation between protein molecules were involved in the aggregation. The average molecular weight of DEW products with alkaline pHs was relatively higher than those with neutral pHs and the same degree of protein unfolding, probably because of more disulfide bond formation between protein molecules. In addition, strong correlations were found between hydrophobicity, surface SH groups plus average molecular weight of DEW-SPA, and physical properties of the gels from DEW products. These data indicated that controlling the aggregation of DEW proteins in the dry state is crucial to controlling the gelling properties of DEW.

Egg white drying: Influence of industrial processing steps on protein structure and functionalities

“…The stiffest gels were obtained when the denaturation temperature, the surface hydrophobicity and the ellipticity of the protein was high, whereas, measurements at 295 nm (fluorescence intensity, maximal emission wavelength, absorbance variation in CD) were low. Parts of these results are in agreement with the literature since Handa et al (2001) showed that gel firmness increased with protein surface hydrophobicity. On the opposite, Kato, Ibrahim, Watanabe, Honma, and Kobayashi (1990) showed that gel firmness increased with the decrease of denaturation temperature and ellipticity of egg white proteins, but they were working on single protein solutions and not with egg white, as in the present study.…”

“…Heating of egg white powder at 75-80°C for 10-15 days is widely used in industry to offset functional property losses resulting from the spray-drying process: both gelling and foaming properties improve after such a dry-heating treatment (Handa, Hayashi, Shidara, & Kuroda, 2001;Kato, Ibrahim, Watanabe, Honma, & Kobayashi, 1989;Mine, 1996). However, it would be interesting to identify the critical steps of the drying process, to understand the mechanisms responsible for the functional property losses in order to limit their harmful effects, and thus to reduce storage time at high temperature.…”

Functional and physicochemical properties of whole egg powder: effect of spray drying conditions

“…1b, higher atomization pressure and outlet air temperature provide to a certain improvement in gelling properties. In general, surface hydrophobicity increases during drying of egg and has a beneficial effect on the gel texture (Kato et al 1990;Handa et al 2001;Baron et al 2003). It was found that the gel texture was not affected significantly by the air inlet temperature ( Table 2).…”

Tri-n-Butylborane/WaterComplex-Mediated Copolymerization of Methyl Methacrylate with Proteinaceous Materials and Proteins: A Review

“…The N-terminal protein is acetylated and contains four cysteine and one cysteine residue [36]. Hydrophobic interactions and disulfide bond formation between ovalbumin molecules is involved in aggregation and surface gelatinization [37]. This structure of ovalbumin may be responsible for the relatively large molecular weight of the grafted-PMMA branches.…”