Selection of a pH- and temperature-stable laccase from Ganoderma australe and its application for bioremediation of textile dyes

被引:35
作者
Si, Jing [1 ]
Wu, Yi [1 ]
Ma, Hong-Fei [1 ]
Cao, Yong-Jia [1 ]
Sun, Yi-Fei [1 ]
Cui, Bao-Kai [1 ,2 ]
机构
[1] Beijing Forestry Univ, Inst Microbiol, Sch Ecol & Nat Conservat, Beijing 100083, Peoples R China
[2] Beijing Forestry Univ, Beijing Adv Innovat Ctr Tree Breeding Mol Design, Beijing 100083, Peoples R China
基金
中国国家自然科学基金;
关键词
Laccase; White rot fungi; Purification; Characterization; Immobilization; Bioremediation; MALACHITE GREEN; PURIFICATION; DEGRADATION; REDUCTION; RESIDUES; ENZYMES; DECOLORIZATION; IMMOBILIZATION; SURFACTANTS; PROTEINS;
D O I
10.1016/j.jenvman.2021.113619
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
By virtue of screening, purification, and properties characterization, this study captures a new pH- and temperature-stable laccase, designated Galacc-F, from Ganoderma australe for dye bioremediating applications. The enzyme was purified to homogeneity by salt precipitation, ionic exchange, and size exclusion chromatography with a final specific activity of 22.214 U mg(-1), yielding a purification fold of 23.989 and recovery of 38.44%. Its molecular weight was estimated to be 48.0 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, zymography, Sephadex G-100 column, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, which confirmed its monomeric nature. Galacc-F exhibited high levels of activity and stability over wide ranges of pH (5.0-8.0) and temperature (10-60 degrees C), which are highly valuable properties in industrial processes. Broad substrate specificity was observed, wherein a better affinity was found for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) with a low value of K-m (164.137 mu M) and higher k(cat)/K-m ratio (1.663 s(-1) mu M-1). Activity was stimulated by Cu2+ and beta-mercaptoethanol but inhibited by ethylenediaminetetraacetic acid, diethylpyrocarbonate, iodoacetic acid, phenylmethylsulfonyl fluoride, and Hg2+, indicating that Galacc-F is a metalloprotease containing a typical histidine-cysteine-serine catalytic triad. It had high tolerance to surfactants, oxidants, and salts. Additionally, a fabricated protocol for native Galacc-F immobilization onto Fe3O4@Chitosan composite nanoparticles using glutaraldehyde as a crosslinker was developed. Most importantly, the enzyme was determined to be ideal for use in efficient treatment of dye effluents as compared with the laccases requiring redox mediators.
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页数:12
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