Amino acid-amidated pectin: Preparation and characterization

There is interest in extending the functionality of natural polymers using simple chemical derivatization methods. In this study, the ability of pectin to react with various amino acids (40 degrees C) in aqueous solution without a catalyst was investigated, including glutamic acid, glycine, cysteine, lysine, and arginine. Only glycine, lysine, and arginine could form conjugates with pectin under these conditions. Amino acid-amidated pectin (AAAP) conjugates with a degree of amidation of 6.50% were prepared and characterized using elemental analysis, FTIR, and H-1 NMR. Size exclusion chromatography combined with multiangle light scattering and refractive index detection indicated pectin degradation occurred during the reaction. These results were supported by measurements of apparent viscosities. Scanning electron microscopy showed appreciable differences among the surface topographies of samples. Cell culture experiments showed the AAAP conjugates exhibited no cytotoxic effects. Our results suggested the AAAP conjugates may be suitable for use as new functional ingredients in food industry.