科研之友
微信
新浪微博
Facebook
分享链接
摘要
This study seeks to clarify the physicochemical properties and aggregation behavior of N-terminal domain of high molecular weight glutenin subunits (HMW-GS) 1Dx5 (1Dx5-N).Effects of edible salts (NaC1, Na2CO3),disulfide bond reductant dithiothreitol (DTT) and hydrophobic interactions of denaturant sodium dodecyl sulfonate (SDS) on 1Dx5-N polymer were investigated by native polyacrylamide gelelectrophoresis (PAGE), nonreducing/reducing SDS-PAGE, intrinsic fluorescence, size exclusion chromatography (SEC), dynamic light scattering (DLS) and circular dichroism (CD).Results showed that 1Dx5-N formed a soluble aggregate in aqueous solutions by native-PAGE, clarifying the role of N-terminal of HMW-GS in the insolubility of the whole subunits.Meanwhile, the hydrophobic interaction was more potent in promoting the aggregation of 1Dx5-N in aqueous solutions from the results of SEC, DLS and CD.Moreover, the hydrophobic interactions could reinforce the formation of covalent bonds between 1Dx5-N.Edible salts, NaC1 and Na2CO3, could improve the polymer formation of 1Dx5-N through disulfide bonds.Additionally, Na2CO3 at high concentrations (>200 mM) induced other types of cross-links between amino acids in 1Dx5-N according to nonreducing/reducing SDS-PAGE and fluorescence spectrum.Therefore, these results provide much novel information on the N-terminal domain of HMW-GS to facilitate the understanding of its functional properties in wheat flour.
- 单位
