Many organisms possess the ability to produce metal-binding proteins to absorb cadmium. Metallothioneins, an important family of cysteine-rich metal-binding proteins, have been isolated and well characterized. However, Lentinula edodes may have a different type of cadmium-binding protein that contains fewer cysteine residues. In the present study, we purified a cadmium-binding protein from L. edodes (LECBP) by gel filtration and anion exchange chromatography and then identified LECBP by LC-MS/MS. We found LECBP to be a novel cadmium-binding protein, which contained 220 amino acid residues but no cysteine residue. LECBP had a high binding affinity for Cd(II) with a Kd value of 97.3 μM. The percentages of α-helix, β-sheet, β-turn, and random coil in LECBP were 15.7%, 39.4%, 8.0%, and 37.1%, respectively. In addition, high temperatures and an acidic environment influenced the conformation of LECBP. Our results will thus provide a new perspective to understand the mechanism of cadmium accumulation in L. edodes.
Keywords: Lentinula edodes; cadmium-binding protein; characterization; identification; purification.