An antifungal protein from the culinary-medicinal beech mushroom, Hypsizygus marmoreus (Peck) Bigel. (Agaricomycetideae).

An antifungal protein (HM-af) was purified from the culinary-medicinal mushroom Hypsizygus marmoreus. The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight mass spectrometry of HM-af indicated that its molecular mass was 9.5 kDa.

Purification, characterization, and sugar binding specificity of an N-Glycolylneuraminic acid-specific lectin from the mushroom Chlorophyllum molybdites.

A carbohydrate-binding protein was isolated from the carpophores of the mushrooms and designated the Chlorophyllum molybdites lectin (CML) based on its origin. The molecular mass of CML was 32 kDa, and it was composed of two 16-kDa monomers with no disulfide bonds. Monosaccharide analysis indicated that 12% of the mass of CML was carbohydrate and consisted of GlcNAc:GalNAc:Gal:Man:l-Fuc in a molar ratio of 1.