文章基本信息

标题：Purification and biochemical characterization of extracellular manganese peroxidase from Ganoderma lucidum IBL-05 and its application
本地全文：下载
作者：Muhammad Bilal ; Muhammad Asgher ; Muhammad Ramzan 等
期刊名称：Scientific Research and Essays
印刷版ISSN：1992-2248
出版年度：2015
卷号：10
期号：14
页码：456-464
DOI：10.5897/SRE2015.6268
语种：English
出版社：Academic Journals
摘要：In this study an extracellular manganese peroxidase (MnP) was isolated from culture filtrate of an indigenous fungal strain Ganoderma lucidum IBL-05 under static conditions using wheat bran as substrate. The enzyme was purified by applying successively ammonium sulphate precipitation, dialysis, ion exchange and gel filtration chromatographic techniques. Purification procedure resulted in 3.43-fold purification with corresponding specific activity of 539.59 Umg-1. The purified MnP elucidated single band in 43 kDa region on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The purified MnP showed optimum activity at pH 5 and 40°C temperature. The Km and Vmax for MnP toward MnSO4 as a substrate were found to be 65.5 mM and 640 UmL-1, respectively. It was observed that MnP activity enhanced by Mn2+ and Cu2+ and inhibited in the presence of Zn2+, Fe2+, EDTA and Cysteine to various extents with Hg2+ (most inhibitory). The purified MnP efficiently catalyzed the transformation of different synthetic textile dyes (Sandal-reactive dyes). Characterization revealed that MnP isolated from G. lucidum have potential to be used for myriad industrial and biotechnological applications.
关键词：Manganese peroxidase; Ganoderma lucidum IBL-05; purification; characterization; kinetics; dye decolorization " />

联系我们|关于我们|网站声明