期刊
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
卷 27, 期 6, 页码 1120-1127出版社
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
DOI: 10.4014/jmb.1701.01004
关键词
Laccase; Marasmius scorodonius; synthetic dyes; decolorization
Marasmius scorodonius secretes an extracellular laccase in potato dextrose broth, and this enzyme was purified up to 206-fold using (NH4)(2)SO4 precipitation and a Hi-trap Q Sepharose column. The molecular mass of the purified laccase was estimated to be similar to 67 kDa by SDSPAGE. The UV/vis spectrum of the enzyme was nontypical for laccases, and metal content analysis revealed that the enzyme contains 1 mole of Fe and Zn and 2 moles of Cu per mole of protein. The optimal pH for the enzymatic activity was 3.4, 4.0, and 4.6 with 2,2'-azino-bis(3ethylbenzothazoline-6-sulfonate) (ABTS), guaiacol, and 2,6-dimethoxy phenol as the substrate, respectively. The optimal temperature of the enzyme was 75 degrees C with ABTS as the substrate. The enzyme was stable in the presence of some metal ions such as Ca2+, Cu2+, Ni2+, Mg2+, Mn2+, Ba2+, Co2+, and Zn2+ at a low concentration (1 mM), whereas Fe2+ completely inhibited the enzymatic activity. The enzymatic reaction was strongly inhibited by metal chelators and thiol compounds except for EDTA. This enzyme directly decolorized Congo red, Malachite green, Crystal violet, and Methylene green dyes at various decolorization rates of 63-90%. In the presence of 1-hydroxybenzotriazole as a redox mediator, the decolorization of Reactive orange 16 and Remazol brilliant blue R was also achieved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据