Article Abstract:
The manganese peroxidase (MnP) isozyme from the hyperlignolytic fungus IZU-154 shows 1.6 times greater lignolytic activity and k(sub cat)/K(sub m) as compared to the MnP from Phanerochaete chrysosporium. This may be due to the discrepancies shown by the two types of MnPs in the context around the distal histidine residue. Two cDNAs encoding MnP isozymes show 96.2% identity at the nucleotide level and 95.1% identity at the amino acid level. The primary structures of the two MnPs from IZU-154 are similar to the MnPs from P. chrysosporium.
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Article Abstract:
Research was conducted to examine the purification and characterization of a nylon-degrading enzyme found in the extracellular medium of a ligninolytic culture of the white rot fungus strain IZU-154. The methodologies used were ion-exchange chromatography, hyrophobic chromatography and gel filtration chromatography. Investigation of the degradation of nylon-6 fiber was also performed. Results indicate that nylon is degraded selectively to soluble oligomers.
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Article Abstract:
Nylon-66 is significantly degraded by the white rot fungus IZU-154, under ligninolytic conditions. Four end groups, CHO, NHCHO, CH3, and CONH2 are formed in the biodegraded nylon-66 membranes, suggesting the involvement of a thermal oxidative degradation mechanism. The white rot fungi have the latent ability to degrade nylon. Nylon degradation is accelerated by the addition of manganese.
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