Abstract
To guide the preparation of protein-based adhesive, especially the soy-based adhesive, the reaction between a simple dipeptide N-(2)-l-alanyl-l-glutamine (AG), being used as a model compound of protein, and its cross-linker furfuryl alcohol were studied in this paper. The products that were prepared with furfuryl alcohol and AG under different pHs were analyzed by ESI-MS, (13)C NMR, and FT-IR. It was found that the medium environment had great effects on the competition of the co-condensation reaction between furfuryl alcohol and AG and self-condensation reaction of furfuryl alcohol molecules in the mixing system with furfuryl alcohol and AG. Under alkaline conditions, both co- and self-condensation were not obviously detected. Only when the value of pH was higher than 11, were a few co-condensation reaction products gotten. The reaction occurred mainly between furfuryl alcohol and the primary amido groups of AG. Under acid conditions, both co- and self-condensation were observed. The more acid the preparation conditions were, the easier to be observed the self-condensation of furfuryl alcohol molecules would be than the co-condensation between furfuryl alcohol and AG. When the value of pH was higher than 5, both co- and self-condensation were not outstanding. In this study, under pH 3, the co- and self-condensation found equilibrium. There was a great possibility for the primary amido and aliphatic amino groups of AG molecules to react with furfuryl alcohol molecules. No reaction was detected between the secondary amido groups of AG and furfuryl alcohol.