Characterization of Multi-Complex Glycoprotein from Abalone

Abstract

An extracellular multi-complex glycoprotein (MCGP) that not able to be fractionated by ammonium sulfate fractionation, anion-exchange chromatography, and gel-filtration chromatography was isolated and its enzyme activity was characterized. The molecular weight of the MCGP was estimated to be 245 kDa based on the SDS-PAGE. The highest substrate specificity of MCGP was determined toward alpha-amylose, which was isolated from the defatted biomass of a microalgae Dunaliella tertiolecta. In addition, moderate enzyme activity was observed toward starch, beta-glucan and alginate compared with the alphaamylose. Lower enzyme activity toward fucoidan and high molecular weight chitosan (HMWC) than other substrates were also observed, showing that MCGP has the multi-substrate specificity. Our results demonstrate the suitability of MCGP for the biocatalysis of high molecular weight polysaccharides with high efficiency to produce shorter chains, which are applicable in various fields such as a food, pharmaceutical and potential use in cosmetic applications.