A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
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منابع مشابه
A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack and solubilize lignin. In this work, we screened 43 filamentous actinomycetes by assaying their a...
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The mechanism by which lignin peroxidase (Lip) interacts with the lignin polymer is discussed. Veratryl alcohol (Valc), a secondary metabolite of white rot fungi, acts as a cofactor for the enzyme. The Lip-redox cycle is discussed in terms of Marcus theory of electron transfer. It is proposed that reaction of a nucleophile in the active site channel with the incipient Valc'. is an essential eve...
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UNLABELLED BACKGROUND The enzymatic hydrolysis step converting lignocellulosic materials into fermentable sugars is recognized as one of the major limiting steps in biomass-to-ethanol process due to the low efficiency of enzymes and their cost. Xylanases have been found to be important in the improvement of the hydrolysis of cellulose due to the close interaction of cellulose and xylan. In t...
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LiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) instead of the tryptophan conserved in other lignin-degrading peroxidases. Pristine LiP showed a lag period in VA (veratryl alcohol) oxidation. However, VA-LiP (LiP after treatment with H2O2 and VA) lacked this lag, and H2O2-LiP (H2O2-treated LiP) was inactive. MS analyses revealed that VA-LiP in...
متن کاملDirect interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium.
Binding properties of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium against a synthetic lignin (dehydrogenated polymerizate, DHP) were studied with a resonant mirror biosensor. Among several ligninolytic enzymes, only LiP specifically binds to DHP. Kinetic analysis revealed that the binding was reversible, and that the dissociation equilibrium constant was 330 micro...
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ژورنال
عنوان ژورنال: Biotechnology Reports
سال: 2017
ISSN: 2215-017X
DOI: 10.1016/j.btre.2016.12.005