In order to obtain a high purity and high biological activity of mannoprotein from S. cerevisiae, the extraction, structural characterization, and antineoplastic activity of mannoprotein were investigated. The mannoprotein was dealt with trichloroacetic acid to remove the protein, and then purified by gel filtration chromatography to the purity of 92.61 ± 0.42%. The molecular weight of the mannoprotein was determined to be 166–700 Da by GPC-LLS. Structural analysis revealed that the mannoprotein was a glycoprotein. The mannan consisted of α-1, 6-glycosidic linkages as the main chains, while some α-1, 2-glycosidic linkages existed as the side chains, and the protein consisted of 17 kinds of amino acids. The atomic force microscopy results showed mannoprotein was composed of many conglobulations. S. cerevisiae mannoprotein exhibited significantly higher inhibition ratios of HepG2, HL-60, and Eca109 cells than degraded S. cerevisiae mannoprotein by proteolytic enzymes.
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