Department of Analytical Chemistry, Ghent University, Krijgslaan 281 S12, B-9000 Ghent, Belgium.
Talanta. 2010 Oct 15;82(5):1980-5. doi: 10.1016/j.talanta.2010.08.019. Epub 2010 Aug 24.
The aim of this paper is to emphasize the strength of gelatin as a stable matrix for redox enzymes. Cyclic voltammetry has been applied for a detailed electrochemical study of horse heart cytochrome c (HHC) entrapped in a gelatin matrix immobilized on a gold electrode. The influence of the HHC concentration, the mass percentage of the gelatin and the nature of the gelatin on the electrochemical behaviour of HHC have been described in detail. In addition, attenuated total reflection infrared (ATR-IR) spectroscopy was used to prove the immobilization on a qualitative and conformational level. The thickness of the gelatin film was determined using a non-contact optical profiler. These results open up new perspectives in the development of stable, biocompatible matrices for redox enzymes. The latter has its relevance in the field of biosensor development.
本文旨在强调明胶作为氧化还原酶稳定基质的优势。循环伏安法已应用于详细的电化学研究，研究了固定在金电极上的明胶基质中包埋的马心细胞色素 c（HHC）。详细描述了 HHC 浓度、明胶的质量百分比和明胶的性质对 HHC 电化学行为的影响。此外，衰减全反射红外（ATR-IR）光谱用于在定性和构象水平上证明固定化。使用非接触式光学轮廓仪确定明胶膜的厚度。这些结果为开发稳定、生物相容的氧化还原酶基质开辟了新的前景。后者在生物传感器开发领域具有相关性。
