Solid state fermentation of Achras zapota lignocellulose by Phanerochaete chrysosporium.
The biological transformation of lignocellulose of Achras zapota by white rot fungi, Phanerochaete chrysosporium, in solid state fermentation (SSF) was studied for 28 days. The kinetic transformation of lignocellulose was monitored through the determination of acid soluble and acid insoluble lignin content, total organic carbon (TOC) and chemical oxygen demand (COD). The lignolytic enzymes, lignin peroxidase (LiP) and manganese peroxidase (MnP) were quantified on weekly intervals. The degradation of lignin and other structural moieties of A. zapota lignocellulose were confirmed by high performance liquid chromatography (HPLC), Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The degradation of lignin was increased after 7 days of fermentation with the release of water soluble and fermentable products. The LiP and MnP activities were increased in the first week of SSF and lignin degradation was also set to increase. This was accompanied with increase in COD by 94.6% and TOC by 80% and lignin content was decreased by 76%. The maximum activities of the enzymes LiP and MnP in extracellular fluid of SSF under nitrogen limitation, at pH 5.0, at temperature 37 degrees C and at 60% humidity were 2100 U/L and 1200 U/L.
Ganesh Kumar
A
A
Department of Environmental Technology, Central Leather Research Institute, Adyar, Chennai, Tamil Nadu, India.
Sekaran
G
G
Krishnamoorthy
Sarayu
S
D001487:Basidiomycota / Q000378:metabolism*; D019149:Bioreactors / Q000382:microbiology*; D018929:Cell Culture Techniques / Q000379:methods*; D002482:Cellulose / Q000378:metabolism*; D003198:Computer Simulation; D005285:Fermentation / Q000502:physiology; D008031:Lignin / Q000378:metabolism*; D032129:Manilkara / Q000382:microbiology*; D008954:Models, Biological; D010544:Peroxidases / Q000378:metabolism*
C036909:lignocellulose; D002482:Cellulose; D008031:Lignin; D010544:Peroxidases; C042858:lignin peroxidase; C051129:manganese peroxidase