title: Decolorization applicability of sol-gel matrix immobilized manganese peroxidase produced from an indigenous white rot fungal strain Ganoderma lucidum.
abstract: BACKGROUND
  An eco-friendly treatment of industrial effluents is a major environmental concern of the modern world in the face of stringent environmental legislations. By keeping in mind the extensive industrial applications of ligninolytic enzymes, this study was performed to purify, and immobilize the manganese peroxidase (MnP) produced from an indigenous strain of Ganoderma lucidum. The present study was also focused on investigating the capability of immobilized MnP for decolorization of dye containing textile effluents.
  
  
  RESULTS
  A large magnitude of an indigenous MnP (882±13.3 U/mL) was obtained from white rot fungal strain G. lucidum in solid state bio-processing of wheat straw under optimized fermentation conditions (moisture, 50%; substrate, 5 g; pH, 5.5; temperature, 30°C; carbon source, 2% fructose; nitrogen source, 0.02% yeast extract; C: N ratio, 25:1; fungal spore suspension, 5 mL and fermentation time period, 4 days). After ammonium sulfate fractionation and Sephadex-G-100 gel filtration chromatography, MnP was 4.7-fold purified with specific activity of 892.9 U/mg. G. lucidum MnP was monomeric protein as evident by single band corresponding to 48 kDa on native and denaturing SDS-PAGE. The purified MnP (2 mg/mL) was immobilized using a sol-gel matrix of tetramethoxysilane (TMOS) and proplytrimethoxysilane (PTMS). The oxidation of MnSO4 for up to 10 uninterrupted cycles demonstrated the stability and reusability of the immobilized MnP. Shelf life profile revealed that enzyme may be stored for up to 60 days at 25°C without losing much of its activity. To explore the industrial applicability of MnP produced by G. lucidum, the immobilized MnP was tested against different textile effluents. After 4 h reaction time, the industrial effluents were decolorized to different extents (with a maximum of 99.2%). The maximally decolorized effluent was analyzed for formaldehyde and nitroamines and results showed that the toxicity parameters were below the permissible limits.
  
  
  CONCLUSIONS
  In conclusion, G. lucidum MnP was immobilized by sol-gel matrix entrapment with an objective to enhance its practical efficiencies. The MnP was successfully entrapped into a sol- gel matrix of TMOS and PTMS with an overall immobilization efficiency of 93.7%. The sol- gel entrapped MnP seems to have prospective capabilities which can be useful for industrial purposes, especially for bioremediation of industrial effluents.
authors.affiliation: Industrial Biotechnology Laboratory, Department of Chemistry and Biochemistry, University of Agriculture, Faisalabad, Pakistan. nasir_pk99@hotmail.com
authors.forename: Hafiz
authors.initials: H
authors.lastname: Muhammad Nasir Iqbal
authors.forename: Muhammad
authors.initials: M
authors.lastname: Asgher
mesh_terms: D001673:Biodegradation, Environmental; D004800:Enzymes, Immobilized / Q000737:chemistry*; D005285:Fermentation; D005557:Formaldehyde / Q000737:chemistry; D005782:Gels; D006863:Hydrogen-Ion Concentration; D010544:Peroxidases / Q000737:chemistry* / Q000302:isolation & purification; D019904:Polymethyl Methacrylate / Q000737:chemistry*; D020940:Reishi / Q000201:enzymology*; D012821:Silanes / Q000737:chemistry; D013696:Temperature; D013783:Textile Industry; D062065:Wastewater / Q000737:chemistry
chemical_list: D004800:Enzymes, Immobilized; D005557:Formaldehyde; D005782:Gels; D010544:Peroxidases; D019904:Polymethyl Methacrylate; D012821:Silanes; D062065:Wastewater; C061205:tetramethoxysilane; C051129:manganese peroxidase