Study On The Reaction Of Water-soluble Epoxy Compound With Collegen Peptide

The research that the epoxy compound reacted with amino acid and protein wereintroduced in this paper. The research focuses on the reaction of water-soluble epoxycompound with collegen peptide. In this paper, the glycidyl was selected to modifythe collegen peptide. In the study, reaction law, kinetics, ultrasound reaction andcopper (Ⅱ) complexation were included.In order to accurately quantitative the conversion rate of glycidyl and collagenpeptide reactions. The primary amino tester was invented to use for measuring theprimary amino of collagen peptide. The feasibility of amino locator has beenvalidated.The conversion rates between glycidyl and collegen peptide was studied by theamino locator. The research condition were concentration, pH, time and temperature.The structure and properties of modified collegen peptide were analyzed by DMA andDSC. The water absorbed and retention of modified collegen peptide were measured.The dynamic model was established following excessive glycidyl. The reactioncondition between glycidyl and collegen peptide were concentration, pH andtemperature. At first, the reaction order of primary amino groups was determined.Then, the reaction order of epoxide groups was determined following6,8,10,12,14and16times more surplus glycidyl. The overall reaction order and the activationenergy was calculated. At last, the reaction mechanism was briefly discussedThe reaction between glycidyl and collegen peptide was studied by ultrasound.The aggregation of collegen peptide solution could be influenced by differentultrasonic power under different concentration of6wt%、10wt%、14wt%. Theconversion rates between glycidyl and collegen peptide was studied under differentultrasonic power.The experiment that copper (Ⅱ) complexed modified collegen peptide wasstudied at last. The complexing ability of different copper (Ⅱ) was measured byultraviolet. The pure collegen peptide complexed an equal copper (Ⅱ) by comparingwith modified collegen peptide. The result was discussed by scanning electronicmicroscope and DSC.