Enhanced Catalytic Potentiality of Ganoderma lucidum IBL-05 Manganese Peroxidase Immobilized on Sol-Gel Matrix

Publication date: Available online 31 March 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Muhammad Bilal, Muhammad Asgher, Muhammad Shahid Sol-gel immobilization is an efficient approach to improve the catalytic and life-time properties of biocatalyst. A monomeric 43kDa manganese peroxidase (MnP) from Ganoderma lucidum IBL-05 was immobilized using hydrophobic sol–gel matrix of tetramethoxysilane and propyltrimethoxysilane. The method led to very effective MnP immobilization (91.0%), and imparted remarkable stability to the enzyme (82.7±0.9% after 2 months of storage at 4°C). The optimum pH was 5.0 and 4.0 for soluble and sol-gel immobilized MnP, respectively. Sol-gel encapsulated MnP exhibited 43% residual activity at 50°C, whereas the free enzyme lost its activity completely after 72h. After 5h reaction time, textile wastewater effluents were decolorized to different extents (with a maximum of 93.92%) by immobilized MnP. Operational stability of the entrapped MnP was significantly improved after immobilization, and it retained more than 70% of original activity after three repeated uses for the tested effluents. The chemical oxygen demand (COD) and total organic carbon (TOC) of maximally decolorized effluents were below the permissible limits. The cytotoxicity evaluated through Allium cepa and brine shrimp lethality tests was considerably reduced after treatment with immobilized MnP. The broader pH stability, better thermo-and storage stab...
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research