AI Article Synopsis

  • - The study explored how moderate electric field (MEF) treatment affects the aggregation of soybean 7S globulin, comparing it to conventional water bath methods.
  • - Results showed that MEF treatment significantly improved solubility, turbidity, and particle size, indicating better aggregate properties than untreated globulin at an electric field strength of 8 V/cm.
  • - Structural analysis revealed that MEF treatment altered the protein's spatial configuration, reducing β-sheet content and exposing buried Try residues, which enhanced surface hydrophobicity and improved foaming properties.

Article Abstract

In this study, the aggregation behaviour of soybean 7S globulin after moderate electric field (MEF) treatment was investigated, and the influence of the electric field and temperature field on the structure and foaming property of the aggregates were analysed and compared with conventional water bath (COV). The results showed that MEF treatment enhanced the properties of the aggregates. The properties of the treated aggregates were significantly better than those of native 7S globulin. At an electric field strength of 8 V/cm, the solubility, turbidity, and particle size increased from 95.81 % to 99.37 %, 0.097 to 0.189 and 61.97 nm to 113.21 nm, respectively, and the absolute value of potential decreased from 23.56 mV to 22.12 mV. The SDS-PAGE and size exclusion chromatography (SEC) results showed that the electric field had a positive effect on the aggregate formation of the Fourier-transform infrared spectroscopy (FTIR), fluorescence spectroscopy, surface hydrophobicity (H) and total sulfhydryl (SH) results indicated that the spatial structure of the protein was changed by MEF treatment. The protein β-sheet content was reduced, and the Try that was originally buried inside the molecule was exposed, resulting in an increase in H and a decrease in SH. The foaming property of the 7S globulin aggregates was improved by MEF treatment.

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Source
http://dx.doi.org/10.1016/j.ijbiomac.2023.125784DOI Listing

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