engineering

Lignin peroxidase

Lignin peroxidase is a engineering topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand Lignin peroxidase rather than just read about it. In short: In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2 ⇌ {\displaystyle \rightleftharpoons } 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H2O Thus, the two substrates of this enzyme are 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol and H2O2, whereas its 3 products are 3,4-dimethoxybenzaldehyde, 1-(…

Key takeaways

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Reference excerpt

In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction

1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2 ⇌ {\displaystyle \rightleftharpoons } 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H2O Thus, the two substrates of this enzyme are 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol and H2O2, whereas its 3 products are 3,4-dimethoxybenzaldehyde, 1-(3,4-dimethoxyphenyl)ethane-1,2-diol, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases) and can be included in the broad category of ligninases. The systematic name of this enzyme class is 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase. Other names in common use include diarylpropane oxygenase, ligninase I, diarylpropane peroxidase, LiP, diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving). It employs one cofactor, heme.

Background Lignin is highly resistant to biodegradation and only higher fungi and some bacteria are capable of degrading the polymer via an oxidative process. This process has been studied extensively in the past twenty years, but the mechanism has not yet been fully elucidated. 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.

Structural studies As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1B80, PDB: 1B82, and PDB: 1B85.

References

K.E.L. Eriksson; R.A. Blanchette; P. Ander (1990). Microbial and Enzymatic Degradation of Wood and Wood Components. Springer-Verlag. Hans E. Schoemaker; Klaus Piontek (1996). "On the interaction of lignin peroxidase with lignin". Pure and Applied Chemistry. 68 (11): 2089–96. doi:10.1351/pac199668112089. S2CID 34951982. Paszczynski A; Huynh VB; Crawford R (1986). "Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium". Arch. Biochem. Biophys. 244 (2): 750–65. doi:10.1016/0003-9861(86)90644-2. PMID 3080953. Renganathan V; Miki K; Gold MH (1985). "Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium". Arch. Biochem. Biophys. 241 (1): 304–14. doi:10.1016/0003-9861(85)90387-X. PMID 4026322. Tien M; Kirk TT (1984). "Lignin-degrading enzyme from Phanerochaete chrysosporium purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase". Proc. Natl. Acad. Sci. USA. 81 (8): 2280–2284. Bibcode:1984PNAS...81.2280T. doi:10.1073/pnas.81.8.2280. PMC 345042. PMID 16593451. Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT (1998). "Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis". Biochemistry. 37 (43): 15097–105. doi:10.1021/bi981633h. PMID 9790672. Wariishi H, Marquez L, Dunford HB, Gold MH (1990). "Lignin peroxidase compounds II and III. Spectral and kinetic characterization of reactions with peroxides". J. Biol. Chem. 265 (19): 11137–42. doi:10.1016/S0021-9258(19)38568-0. PMID 2162833. Cai DY, Tien M (1990). "Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies". Biochemistry. 29 (8): 2085–91. doi:10.1021/bi00460a018. PMID 2328240. Tien M, Tu CP (1987). "Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium". Nature. 326 (6112): 520–3. Bibcode:1987Natur.326..520T. doi:10.1038/326520a0. PMID 3561490. S2CID 4321253. Renganathan V, Miki K, Gold MH (1986). "Role of molecular oxygen in lignin peroxidase reactions". Arch. Biochem. Biophys. 246 (1): 155–61. doi:10.1016/0003-9861(86)90459-5. PMID 3754412. Kersten PJ, Tien M, Kalyanaraman B, Kirk TK (1985). "The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes". J. Biol. Chem. 260 (5): 2609–12. doi:10.1016/S0021-9258(18)89401-7. PMID 2982828. Kirk TK, Farrell RL (1987). "Enzymatic "combustion": the microbial degradation of lignin". Annu. Rev. Microbiol. 41: 465–505. doi:10.1146/annurev.mi.41.100187.002341. PMID 3318677.

Worked examples

Example 1 — a first encounter with Lignin peroxidase

Start with the simplest possible case. Write down what Lignin peroxidase claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In engineering, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Lignin peroxidase before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Lignin peroxidase ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Lignin peroxidase

In research: Lignin peroxidase appears in engineering research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry: Engineering practice reuses Lignin peroxidase in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom: Lignin peroxidase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 1.11.1, Enzymes of known structure, Heme enzymes, so understanding it makes those chapters shorter.
In everyday life: Look for Lignin peroxidase outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

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How to study Lignin peroxidase in 20 minutes

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Frequently asked questions

What is Lignin peroxidase in simple terms?

In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2 ⇌ {\displaystyle \rightleftharpoons } 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H2O Thus, the two substrates of this enz…

Why does Lignin peroxidase matter?

Because it connects several engineering ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Lignin peroxidase?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Lignin peroxidase.