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Study on the Selective Adsorption of Lignin from Corn Stover Hydrolysate Using Protein Complex and Its Mechanism
Received:September 24, 2025  Revised:November 07, 2025
DOI:10.11981/j.issn.1000-6842.2026.02.95
Key Words:corn stover hydrolysate;lignin removal;protein complex;selective adsorption;mechanism
Author NameAffiliationPostcode
WANG Yifan* College of Light Industry Science and Engineering, Tianjin Key Lab of Pulp and Paper, Tianjin University of Science and Technology, Tianjin, 300457 300457
KONG Lingyi College of Light Industry Science and Engineering, Tianjin Key Lab of Pulp and Paper, Tianjin University of Science and Technology, Tianjin, 300457 300457
LI Xiao College of Light Industry Science and Engineering, Tianjin Key Lab of Pulp and Paper, Tianjin University of Science and Technology, Tianjin, 300457 300457
YU Menghui College of Light Industry Science and Engineering, Tianjin Key Lab of Pulp and Paper, Tianjin University of Science and Technology, Tianjin, 300457 300457
WANG Gaosheng* College of Light Industry Science and Engineering, Tianjin Key Lab of Pulp and Paper, Tianjin University of Science and Technology, Tianjin, 300457 300457
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Abstract:
      In this study, a protein complex composed of egg white protein and soy protein isolate was used to adsorb the lignin in the hydrolysate obtained by the hydrothermal pretreatment of corn stover, and the effectiveness and mechanism of the protein complex in selective adsorption of lignin from the hydrolysate were investigated. The results showed that at reaction temperature of 95 ℃, pH value of 5, and a protein complex dosage of 1.5 g/L, the removal rate of macromolecular lignin reached 89.6%, the removal rate of small molecular lignin was 26.1%, and the total sugar loss was only 0.98%, indicating that the protein complex could preferentially remove macromolecular lignin while exerting minimal influence on sugars. Mechanism analysis revealed that the binding between the proteins and lignin was primarily driven by hydrogen bonding and hydrophobic interactions. As the reaction temperature increased, the degree of protein cross-linking increased, leading to the formation of larger aggregates with enhanced hydrophobicity, which further improved its lignin removal ability.
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