Probing Conformational Change of Bovine Serum Albumin–Dextran Conjugates under Controlled Dry Heating

Abstract

The time-dependent conformational change of bovine serum album (BSA) during Maillard reaction with dextran under controlled dry heating has been studied by small-angle X-ray scattering, fluorescence spectroscopy, dynamic light scattering, and circular dichroism analysis. Through the research on the radii of gyration (Rg), intrinsic fluorescence, and secondary structure, conjugates with dextran coating were found to inhibit BSA aggregation and preserve the secondary structure of native BSA against long-time heat treatment during Maillard reaction. The results suggested that the hydrophilic dextran was conjugated to the compact protein surface and enclosed it and more dextran chains were attached to BSA with the increase of the heating time. The study presented here will be beneficial to the understanding of the conformational evolution of BSA molecules during the dry-heating Maillard reaction and to the control of the protein-polysaccharide conjugate structure.

Synthetic surfactant- and cross-linker-free preparation of highly stable lipid-polymer hybrid nanoparticles as potential oral delivery vehicles

“…The native BSA molecule showed a strong and clear band at 66 kDa, corresponding to the molecular weight of native BSA. In addition, the native BSA also exhibited several smear bands at higher molecular weights ranging from 150 to 300 kDa, which could be due to the impurities or aggregates of BSA monomers during heating process of sample preparation for SDA-PAGE 26–28 . Maillard reaction between BSA and dextran had a prominent effect on the molecular weight profile.…”

Improved heat stability of protein solutions and O/W emulsions upon dry heat treatment of whey protein isolate in the presence of low-methoxyl pectin

“…Several authors observed that conjugation of proteins and polysaccharides through Maillard reaction can minimize the structural loss of the protein by protein aggregation during dry heat treatment (Spotti, et al, 2014;Y. Sun, Hayakawa, & Izumori, 2004;Xia, et al, 2015). In fact, aggregation and Maillard reaction can happen simultaneously and it was reported previously that BSA aggregation upon dry heating can be reduced in the presence of Dextran since it can prevent extra aggregation of BSA (Xia, et al, 2015).…”

“…The latter could be due to the steric hindrance of the LMP which was already attached to WPI. Upon dry heating of BSA with dextran, it was found that a steady state reaction was obtained due to the hindrance from the dextran attached in the BSA (Xia, et al, 2015).…”

“…Sun, Hayakawa, & Izumori, 2004;Xia, et al, 2015). In fact, aggregation and Maillard reaction can happen simultaneously and it was reported previously that BSA aggregation upon dry heating can be reduced in the presence of Dextran since it can prevent extra aggregation of BSA (Xia, et al, 2015). Furthermore, the author suggested that in the presence of Dextran, the amino acids containing the sulfhydryl group responsible for protein aggregation via disulfide bond formation are involved in the Maillard reaction, thus preventing aggregation between proteins.…”

“…Thus, combining the properties of WPI and polysaccharides can be a good way to modify the properties of WPI resulting in a molecule with improved functionality (Dickinson & Galazka, 1991). It has been reported that the presence of polysaccharides enables WPI to minimize structural losses during heating due to the steric force obtained from the polysaccharides (Dickinson, 1993;Dickinson, et al, 1992;Xia, et al, 2015).…”