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Structural Characterization and Properties of Modified Soybean Meal Protein via Solid-State Fermentation by Bacillus subtilis .

Authors :
Miao X
Niu H
Sun M
Li D
Hua M
Wang J
Su Y
Source :
Molecules (Basel, Switzerland) [Molecules] 2023 Dec 08; Vol. 28 (24). Date of Electronic Publication: 2023 Dec 08.
Publication Year :
2023

Abstract

Soybean meal (SBM) is a high-quality vegetable protein, whose application is greatly limited due to its high molecular weight and anti-nutritional properties. The aim of this study was to modify the protein of soybean meal via solid-state fermentation of Bacillus subtilis . The fermentation conditions were optimized as, finally, the best process parameters were obtained, namely fermentation temperature of 37 °C, inoculum amount of 12%, time of 47 h, and material-liquid ratio of 1:0.58, which improved the content of acid-soluble protein. To explore the utilization of modified SBM as a food ingredient, the protein structure and properties were investigated. Compared to SBM, the protein secondary structure of fermented soybean meal (FSBM) from the optimal process decreased by 8.3% for α-helix content, increased by 3.08% for β-sheet, increased by 2.71% for β-turn, and increased by 2.51% for random coil. SDS-PAGE patterns showed that its 25-250 KDa bands appeared to be significantly attenuated, with multiple newborn peptide bands smaller than 25 KDa. The analysis of particle size and zeta potential showed that fermentation reduced the average particle size and increased the absolute value of zeta potential. It was visualized by SEM and CLSM maps that the macromolecular proteins in FSBM were broken down into fragmented pieces with a folded and porous surface structure. Fermentation increased the solubility, decreased the hydrophobicity, increased the free sulfhydryl content, decreased the antigenicity, improved the protein properties of SBM, and promoted further processing and production of FSBM as a food ingredient.

Details

Language :
English
ISSN :
1420-3049
Volume :
28
Issue :
24
Database :
MEDLINE
Journal :
Molecules (Basel, Switzerland)
Publication Type :
Academic Journal
Accession number :
38138505
Full Text :
https://doi.org/10.3390/molecules28248015