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A study was made to find out how important the role of protein binding was in an admixture of syrups of Alimezine (Ali.) (containing new coccine as a coloring matter), Inolin (Ino.) and Leftose (Lef.), which became discolored during the storage of 5.5 hr at room temperature.The discoloration of new coccine in the Ali.symp from red (λmax 510nm) to yellow (λmax445 nm) was monitered at 510 nm nusing a photospectrometer. The acceleration effect on discoloration was found out with Ali. syrup, Ino. syrup and a substitute for Lef. in which lysozyme chloride was replaced by bovine serum albumin (BSA), poly-Llysine and chitosan. The discoloration was reduced with Ali.syrup, Ino.syrup, and water solution of poly-L-glutamic acid and L-lysine, a substitute for Lef. The discoloration of new coccine was not observed in the admixture of 0.01% new coccine, 0.1% Na2SO3 and 0.5% lysozyme chloride in the solution of the 0.01% sodium lauryl sulfate and 1M sodium chloride. It is considered that the interaction of ionic binding between sulfonic group on the new coccine molecular and lysine residual group on the lysozyme chloride is an important factor for discoloration process. The reaction rate of discoloration in the syrup admixture is accelerated by protein binding of new coccine to the lysozyme chloride. The enzymatic activity of lysozyme chloride was not decreased with protein binding or discoloration of new coccine. The profile of electrophoresis of lysozyme chloride and BSA obtained after discoloration in the syrup admixture showed the same profile as that of standard samples.

The Acceleration Effect on Discoloration of New Coccine with Lysozyme in the Admixture of Alimezine Syrup, Inolin Syrup and Leftose Syrup.