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Updated: May 12, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Optimized antioxidant peptides fractions preparation and secondary structure analysis by MIR
Songyi Lin1, Jia Wang, Ping Zhao
1Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China.
Abstract:
The soybean protein was hydrolyzed by Alcalase Food grade (FG) 2.4 L and the optimal hydrolysis parameters of strongest antioxidant capacity of peptides were obtained using response surface methodology (RSM). The effects of reaction temperature, pH value and ratio of enzyme/soybean protein powder ([E/S]) on the 2,2-diphenyl-1-picrylhydrazyl (DPPH) of the peptides was well fitted to a quadric equation with high determination coefficients. The hydrolysate with optimal DPPH was predicted to be obtained at: temperature of 50°C, pH value of 10.32, and [E/S] ratio of 12%. The hydrolysates were separated by the ultrafiltration membranes in the cut-off MW at 1kDa, 3kDa, 10kDa and 30kDa and molecular weight cut-offs (MWCO) I-V were determined antioxidant activity. And secondary structures of those fractions were investigated by mid-infrared spectroscopy (MIR).
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