کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1355372 980853 2007 15 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characterization of two new multiforms of Trametes pubescens laccase
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
پیش نمایش صفحه اول مقاله
Characterization of two new multiforms of Trametes pubescens laccase
چکیده انگلیسی

Electrochemical properties of two multiforms of laccase from Trametes pubescens basidiomycete (LAC1 and LAC2) have been studied. The standard redox potentials of the T1 sites of the enzymes were found to be 746 and 738 mV vs. NHE for LAC1 and LAC2, respectively. Bioelectroreduction of oxygen based on direct electron transfer between each of the two forms of Trametes pubescens laccase and spectrographic graphite electrodes has been demonstrated and studied. It is concluded that the T1 site of laccase is the first electron acceptor, both in solution (homogeneous case) and when the enzymes are adsorbed on the surface of the graphite electrode (heterogeneous case). Thus, the previously proposed mechanism of oxygen bioelectroreduction by adsorbed fungal laccase was additionally confirmed using two forms of the enzyme. Moreover, the assumed need for extracellular laccase to communicate directly and electronically with a solid matrix (lignin) in the course of lignin degradation is discussed. In summary, the possible roles of multiforms of the enzyme based on their electrochemical, biochemical, spectral, and kinetic properties have been suggested to consist in broadening of the substrate specificity of the enzyme, in turn yielding the possibility to dynamically regulate the process of lignin degradation according to the real-time survival needs of the organism.

Electrochemical properties of two new multiforms of laccase from Trametes pubescens basidiomycete are presented. The previously proposed mechanism of oxygen bioelectroreduction by adsorbed fungal laccase was additionally confirmed. The assumed need for extracellular laccase to communicate directly and electronically with a solid matrix (lignin) during the course of lignin degradation is discussed and the possible role of multiforms of the enzyme is suggested.Figure optionsDownload as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic Chemistry - Volume 35, Issue 1, February 2007, Pages 35–49
نویسندگان
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