Mazur M, Krysiński P, Michota-Kamińska A, Bukowska J, Rogalski J, Blanchard G J
University of Warsaw, Department of Chemistry, 02-093 Warsaw, Pasteura 1, Poland.
Bioelectrochemistry. 2007 Sep;71(1):15-22. doi: 10.1016/j.bioelechem.2006.12.006. Epub 2007 Jan 13.
In this paper we present a simple method allowing for stable laccase immobilization on various conducting surfaces that retains the activity of the enzyme. The strategy for laccase immobilization presented in this paper relies on Zr(4+) ion coordination chemistry that involves -COO- terminal groups present on the protein. Using a host of techniques, including surface plasmon resonance (SPR), quartz crystal microbalance (QCM) gravimetry, atomic force microscopy (AFM), surface enhanced Raman scattering (SERS), resonance Raman scattering (RR) and electrochemical techniques, we show that laccase bound to a surface coordinatively through zirconium phosphonate/carboxylate (ZPC) functionalities forms a stable enzymatic layer with the enzyme retaining its activity to a significant extent.
在本文中，我们提出了一种简单的方法，可将漆酶稳定固定在各种导电表面上，并保持酶的活性。本文提出的漆酶固定化策略依赖于Zr(4+)离子配位化学，该化学涉及蛋白质上存在的-COO-末端基团。通过一系列技术，包括表面等离子体共振(SPR)、石英晶体微天平(QCM)重量法、原子力显微镜(AFM)、表面增强拉曼散射(SERS)、共振拉曼散射(RR)和电化学技术，我们表明，通过锆膦酸盐/羧酸盐(ZPC)官能团与表面配位结合的漆酶形成了一个稳定的酶层，且酶在很大程度上保留了其活性。
