期刊
PLOS ONE
卷 9, 期 10, 页码 -出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0110834
关键词
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资金
- Natural Science Foundation of China [41306120]
- Oceanic Public Welfare Industry Special Research Project of China [201305015]
- State Key Laboratory of Pollution Control and Resource Reuse Foundation [PCRRF12011]
- Fujian Provincial Development and Reform Commission Bio-industry Special Project [[2011]1598]
- Fuzhou Science and Technology Bureau [2012-G-125]
Laccases (EC 1.10.3.2) are a class of multi-copper oxidases with important industrial values. A basidiomycete strain Cerrena sp. HYB07 with high laccase yield was identified. After cultivation in the shaking flask for 4 days, a maximal activity of 210.8 U mL(-1) was attained. A 58.6-kDa laccase (LacA) with 7.2% carbohydrate and a specific activity of 1952.4 U mg(-1) was purified. 2,2'-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) was the optimal substrate, with K-m and k(cat) being 93.4 mu M and 2468.0 s(-1), respectively. LacA was stable at 60 degrees C, pH 5.0 and above, and in organic solvents. Metal ions Na+, K+, Ca2+, Mg2+, Mn2+, Zn2+ enhanced LacA activity, while Fe2+ and Li+ inhibited LacA activity. LacA decolorized structurally different dyes and a real textile effluent. Its gene and cDNA sequences were obtained. Putative cis-acting transcriptional response elements were identified in the promoter region. The high production yield and activity, robustness and dye decolorizing capacity make LacA and Cerrena sp. HYB07 potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment.
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