文献类型： 外文期刊
作者： Dong, Xiao-bo 1 ; Liu, Ying 1 ; Feng, Xi 3 ; Shi, Defang 1 ; Bian, Yin-bing 2 ; Ibrahim, Salam A. 5 ; Huang, Wen 1 ;
作者机构： 1.Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Hubei, Peoples R China
2.Huazhong Agr Univ, Inst Appl Mycol, Wuhan 430070, Hubei, Peoples R China
3.Calif State Univ, Dept Nutr Food Sci & Packaging, San Jose, CA 95192 USA
4.Hubei Acad Agr Sci, Res Inst Agr Prod Proc & Nucl Agr Technol, Wuhan 430064, Hubei, Peoples R China
5.North Carolina A&T State Univ, Dept Family & Consumer Sci, 171 Carver Hall, Greensboro, NC 27411 USA
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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