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Lignin is found to be degraded by enzyme lignin peroxidases produced by some fungi like Phanerochaete chrysosporium. The mechanism by which lignin peroxidase (LiP) interacts with the lignin polymer involves veratrole alcohol, which is a secondary metabolite of white rot fungi that acts as a cofactor for the enzyme.
Production of lignin-peroxidase and manganese-peroxidase is the hallmark of basidiomycetes and is often used to assess basidiomycete activity, especially in biotechnology applications. [38] Most white-rot species also produce laccase, a copper-containing enzyme that degrades polymeric lignin and humic substances. [39]
Lignin-modifying enzymes benefit industry as they can break down lignin; a common waste product of the paper and pulp industry. These enzymes have been used in the refinement of poplar as lignin inhibits the enzymatic hydrolysis of treated poplar and Lignin-modifying enzymes can efficiently degrade the lignin thus fixing this problem. [4]
Although MnP, like other lignin peroxidases, is a Class II peroxidase, it has a similar tertiary structure to prokaryotic Class I peroxidases, but contains disulfide bridges like the Class III peroxidases in plants. [8] MnP has a globular structure containing 11-12 α-helices, depending on the species it is produced in.
Only later would peroxidases acquire the ability use a tryptophanyl radical, interacting with a bulky polymer at the surface of the peroxidase, to attack non-phenolic lignin. These findings highlight the importance of taking plant evolution into account when analyzing the evolution of white-rot fungus.
A solution of hydrochloric acid and phloroglucinol is used for the detection of lignin (Wiesner test). A brilliant red color develops, owing to the presence of coniferaldehyde groups in the lignin. [44] Thioglycolysis is an analytical technique for lignin quantitation. [45] Lignin structure can also be studied by computational simulation. [46]
For example, laccases play a role in the formation of lignin by promoting the oxidative coupling of monolignols, a family of naturally occurring phenols. [ 1 ] [ 2 ] Other laccases, such as those produced by the fungus Pleurotus ostreatus , play a role in the degradation of lignin, and can therefore be classed as lignin-modifying enzymes . [ 3 ]
Oxyporus latemarginatus produces the industrially significant enzymes lignin peroxidase and manganese peroxidase (but not laccase), [9] which are used in bioremediation, biopulping, and biobleaching. The fungus was investigated for its ability to degrade lignin in kenaf (Hibiscus cannabinus) chips. [10]
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