•  
  •  
 

Section

Biological Sciences

Abstract

Lignocellulosic enzymes from Crepidotus variabilis collected from mangrove forests of coastal Tanzania were investigated by using standard methods, and their ability to degrade aromatic compounds were elucidated. The fungal crude enzyme filtrates had maximum laccase (Lac), lignin peroxidase (LiP) and manganese peroxidase (MnP) activities of 70 U/mL, 16 U/mL and 8, U/mL respectively. The crude enzyme extracts were able to oxidize rhemazol brilliant blue-R (RBB-R) dye, phenol, "-naphthol and pyrogallol. Also, they could remove up to 58% and 92% color from raw textile effluent and aromatic dyes, respectively, after 14 days of incubation at 30ºC and pH 4.5. Desalted and size-separated enzyme filtrates, resolved by sodium docecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing (IEF), showed laccases and peroxidases from C. variabilis to have molecular weights of 67 kDa and 47 kDa, respectively, while the isoelectric points (pI) of laccases and peroxidases were found to lie in a range of 3.0 to 4.1. The study provided basic information on the characteristics of crude lignolytic enzymes from C. variabilis and confirmed it to be one of the potential biodegraders of aromatic compounds that could be applied in bioremediation of polluted ecosystem.

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.