Surface-engineered Saccharomyces cerevisiae cells displaying redesigned CadR for enhancement of adsorption of cadmium (II)

被引:17
作者
Tao, Hu-Chun [1 ]
Li, Peng-Song [1 ]
Liu, Qi-Song [2 ]
Su, Jie [1 ]
Qiu, Guo-Yu [1 ]
Li, Zi-Gang [2 ]
机构
[1] Peking Univ, Shenzhen Grad Sch, Sch Environm & Energy, Key Lab Heavy Met Pollut Control & Reutilizat, Shenzhen 518055, Peoples R China
[2] Peking Univ, Shenzhen Grad Sch, Sch Chem Biol & Biotechnol, Key Lab Chem Genom, Shenzhen 518055, Peoples R China
基金
美国国家科学基金会;
关键词
cell-surface display; Saccharomyces cerevisiae; CadR; biosorption; cadmium; SWISS-MODEL; MERR FAMILY; YEAST; BIOSORPTION; REMOVAL; ION; METALLOTHIONEIN; BIOADSORPTION; ENVIRONMENT; TITRATION;
D O I
10.1002/jctb.4783
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
BACKGROUND: The use of cell-surface display technology to express recombinant proteins on a microbial cell surface can enhancemetal adsorption to microbial cells. The transcription factor CadR of Pseudomonasputida shows highly selective affinity with Cd2+. RESULTS: CadR was genetically engineered by truncating 47 N-terminal amino acids and 21 C-terminal amino acids in order to maximize its expression efficiency while maintaining its metal-binding domain. The redesigned CadR (named T68CadR) was then displayed with Saccharomyces cerevisiae a-agglutinin cell-surface display system. This engineering approach enhanced the H+/OH- buffering capacity and the Cd2+ adsorption capacity of yeast cells. The surface-engineered cells also performed well at mesophilic and higher temperatures (30-50 degrees C) under neutral or alkalescent conditions. With an initial concentration of 1.0 mg L-1, the Cd2+ removal efficiency remained 85% when the concentration of Na+ changed from 0 to 400 mmol L-1 (pH 7.8). The surface-engineered cells also showed highly selective adsorption to Cd2+ in the presence of Zn2+ and Pb2+. CONCLUSIONS: T68CadR displayed yeast cells constructed in this study provide an option to selectively remove Cd in water. It also might be promising as a tool to determine CadR's Cd-binding mechanism and to improve its selectivity and affinity to Cd2+. (C) 2015 Society of Chemical Industry
引用
收藏
页码:1889 / 1895
页数:7
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