Purification and Characterization of a Cadmium-Binding Protein from Lentinula edodes

文献类型： 外文期刊

第一作者： Dong, Xiao-bo

作者： Dong, Xiao-bo;Liu, Ying;Shi, Defang;Huang, Wen;Bian, Yin-bing;Feng, Xi;Shi, Defang;Ibrahim, Salam A.

作者机构：

关键词： Lentinula edodes; cadmium-binding protein; purification; identification; characterization

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2019 年 67 卷 4 期

页码：

收录情况： SCI

摘要： 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 K-d value of 97.3 mu M. The percentages of alpha-helix, beta-sheet, beta-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.

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