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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.
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]
The systematic name of this enzyme class is Mn(II):hydrogen-peroxide oxidoreductase. Other names in common use include peroxidase-M2, and Mn-dependent (NADH-oxidizing) peroxidase. It employs one cofactor, heme. This enzyme needs Ca 2+ for activity. White rot fungi secrete this enzyme to aid lignin degradation.
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]
It is thought that catalase-peroxidase provides protection to cells under oxidative stress. [5] Class II consists of secretory fungal peroxidases: ligninases, or lignin peroxidases (LiPs), and manganese-dependent peroxidases (MnPs). These are monomeric glycoproteins involved in the degradation of lignin. In MnP, Mn 2+ serves as the reducing ...
Bacteria do not express any of the plant-type peroxidases (lignin peroxidase, Mn peroxidase, or versatile peroxidases), but three of the four classes of DyP are only found in bacteria. In contrast to fungi, most bacterial enzymes involved in lignin degradation are intracellular, including two classes of DyP and most bacterial laccases. [34]
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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