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Updated: Oct 16, 2025

Preparation and Testing of Plant Seed Meal-based Wood Adhesives
Published on: March 5, 2015
Physicochemical, structural and adhesion properties of walnut protein isolate-xanthan gum composite adhesives using
Yuqing Lei1, Sihai Gao2, Xiaole Xiang3
1Engineering Research Center of Bio-process, Ministry of Education/Key Laboratory for Agricultural Products Processing of Anhui Province/School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, China; Key Laboratory of Fermentation Engineering, Ministry of Education/School of Food and Biological Engineering, Hubei University of Technology, Wuhan 430068, China.
Abstract:
Low-sugar and high-protein adhesives have broad market application prospects, while natural plant proteins have confronted technical bottlenecks due to their poor adhesion. In this study, the effects of ethanol with different concentrations (0-80%) on the adhesion properties of walnut protein isolate-xanthan gum (WNPI-XG) composite adhesives were investigated. Results showed the bonding strength of WNPI-XG treated with 40% ethanol reached 12.55 MPa, the denaturation temperature and the surface hydrophobicity increased to 87.91 and 185.07 respectively, displaying the best rheological and texture properties. It also indicated appropriate concentration of ethanol (40%) didn't change the molecular weight of WNPI-XG, but greatly strengthened the fluorescence intensity, leading changes in contents of reactive sulfhydryl groups, electrostatic forces, hydrophobic interactions, hydrogen bonds and disulfide bonds. Furthermore, the treatment also facilitated a conformation conversion of the secondary structures from β-sheet to α-helix, promoting the full unfolding of protein molecules. The microstructure analysis showed after 40% ethanol treatment, the WNPI structure was uniform, the surface of WNPI-XG adhesive was flat and smooth, combined more closely with water molecules. By analyzing the influence of ethanol treatment on adhesion of WNPI-XG, the research laid a theoretical foundation for protein modification, providing good technical references for its development and utilization.

