Peroxidase, Lignin , CAS No.93792-13-3

CAS: 93792-13-3 Cat. No.: P1437472

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Übersicht

Peroxidase, Lignin is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on enhancing enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions such as low or high pH. By introducing stimulus responsiveness to these enzyme modifications, dynamic control of activity is also possible.

Specifications

Storage

Store at -20°C

Verschickt in

Ice chest + Ice pads

Dieses Produkt erfordert Kühlkettenversand. Grundversand und andere Economy-Optionen sind nicht verfügbar.

Application Protocols

No manufacturer-validated application protocols are specified for this item; refer to the product CoA/Spec Sheet. For general assay concepts with lignin peroxidase, consult the primary literature and standard enzymology texts. The supplier does not provide tested conditions or recommended dilutions for this SKU.

Biological Roles

General/literature context (not item-specific):

• Ecological function: Lignin peroxidase is produced by certain white-rot fungi as part of the ligninolytic enzyme system that mineralizes lignin, a recalcitrant component of plant cell walls. It enables carbon cycling in forest ecosystems by breaking down nonphenolic lignin structures.
• Catalytic role: Uses H2O2 to generate high-potential oxidizing intermediates (Compound I/II), capable of abstracting electrons from substrates with oxidation potentials exceeding those of laccases or Mn peroxidases.
• Synergy: Functions synergistically with manganese peroxidase (MnP), versatile peroxidase (VP), aryl alcohol oxidase, and glucose oxidase, which help supply H2O2 and expand substrate scope.
• Substrates/products: Oxidizes nonphenolic aromatics, polycyclic aromatic hydrocarbons, and lignin model dimers; reactions can include Cα–Cβ cleavage, demethoxylation, and aromatic ring opening leading to smaller aromatic aldehydes/acids under subsequent reactions.
• Structural biology: Class II secreted fungal peroxidase with a conserved heme pocket; extracellular glycosylation contributes to stability in acidic, oxidative environments.

Relevance to research:

• Model for studying long-range electron transfer and high-redox-potential biocatalysis.
• Tool enzyme in biotechnology for lignocellulosic biomass valorization, pollutant transformation, and green oxidation method development.

No medical/clinical roles are claimed or implied. This product is for research use only.

Buffer Applications

Item-specific buffer formulation is not specified for this product; consult the CoA/Spec Sheet for the supplied matrix and any recommended reconstitution buffer.

General/literature guidance for buffers with lignin peroxidase (not item-specific):

• pH range: Acidic conditions favor activity for many LiP isoforms (commonly pH 2.5–4 for veratryl alcohol assays). Stability may vary—verify for your preparation.
• Common buffers:
  • Sodium tartrate (e.g., 50 mM, pH 3.0)
  • Citrate or citrate–phosphate mixtures (e.g., 50–100 mM, pH 3.0–4.0)
  • Acetate (25–50 mM, pH ~4), as compatible with your assay readout
• Ionic strength: Moderate ionic strength can stabilize the enzyme; avoid high salt if it interferes with substrate binding or spectroscopy.
• Additives: 5–20% glycerol can improve storage stability in solution; small amounts of Ca2+ sometimes stabilize fungal peroxidases (literature). Avoid EDTA or strong chelators unless required.
• H2O2 handling: Prepare fresh, dilute peroxide in buffer; add gradually (e.g., syringe pump) to maintain low steady-state levels and prevent inactivation.

Assay recipe example (conceptual, literature; not a specification): 50 mM sodium tartrate buffer pH 3.0, 2 mM veratryl alcohol, enzyme at defined units, initiate with 100–200 µM H2O2; monitor A310 for veratraldehyde formation. Adjust concentrations to your enzyme’s specific activity.

Green Alternatives

Context: Lignin peroxidase enables oxidative transformations in water at ambient temperatures, offering a biocatalytic alternative to harsh chemical oxidants.

Comparison of oxidative methods (literature; not item-specific):

• Lignin peroxidase (this class)

  • Oxidant: H2O2 (water byproduct)
  • Medium: Aqueous, acidic
  • Selectivity: High for nonphenolic/high-redox-potential aromatics via radical pathways
  • Tradeoffs: Sensitive to H2O2 spikes; requires careful dosing and pH control

• Laccase (O2 oxidant)

  • Oxidant: O2 (H2O byproduct)
  • Medium: Typically near-neutral to acidic
  • Pros: No external peroxide; milder handling
  • Tradeoffs: Lower redox potential; often requires mediators for nonphenolics

• Chemical oxidants (e.g., MnO2, Cr(VI), peracids)

  • Pros: Robust, simple setups
  • Tradeoffs: Hazardous waste, over-oxidation, poor selectivity, non-aqueous conditions frequent

Greener practice tips (general):

• Generate H2O2 in situ (e.g., glucose oxidase + glucose) to minimize waste and improve enzyme longevity.
• Use recyclable mediator systems (e.g., veratryl alcohol) at catalytic levels where applicable.
• Favor buffered water with minimal organic cosolvent; apply phase-transfer strategies (cyclodextrins, emulsions) over high solvent loads.
• Implement enzyme immobilization or carrier binding to enhance reuse and reduce protein waste.

Note: Specific environmental metrics (E-factor, PMI) for this SKU are not specified; assess at process scale.

Pharmaceutical Uses

No pharmacopeial status, excipient role, or cGMP manufacturing grade is specified for this item; refer to the CoA/Spec Sheet.

General notes (not item-specific):

• Lignin peroxidase is primarily a research and industrial biocatalyst rather than a pharmaceutical excipient. Typical uses are in biotransformations, analytical assays, and environmental applications.
• If considering use in regulated contexts (diagnostics, manufacturing aids), additional qualification would be necessary (e.g., defined activity, impurity profile, bioburden/endotoxin, adventitious agents). This product is labeled For research use only.
• Formulation compatibility: Proteins with heme cofactors can be sensitive to surfactants and preservatives; any integration into device coatings or sensor matrices requires empirical stability testing under the target conditions.

No therapeutic or clinical claims are made or implied for this SKU.

Physical Properties

Item-specific physico-chemical specifications: Not specified for this item; refer to CoA/Spec Sheet.

General/literature properties for lignin peroxidase preparations (not item-specific):

• Physical state: Typically supplied as a lyophilized powder or as an aqueous solution/concentrate; appearance depends on formulation and stabilizers (literature).
• Protein nature: Glycoprotein enzyme containing a ferric heme cofactor; colored solutions may appear light brown to reddish-brown due to the heme chromophore (literature).
• Solubility: Readily soluble in aqueous buffers; insoluble in nonpolar organic solvents. Activity can be sensitive to organic cosolvents above low percentages (literature).
• pH profile: Acidic pH optima are common (often around pH 2.5–4 for veratryl alcohol oxidation, literature). Stability windows can differ from activity optima.
• Temperature profile: Retains activity at ambient to moderate temperatures; prolonged exposure to elevated temperatures promotes denaturation (literature).
• Extinction coefficients and precise activity units depend on isoform and assay (not specified for this item).

Do not interpret any of the above as product specifications. When planning experiments, verify the exact formulation (buffer salts, stabilizers, preservatives), protein concentration, and activity definition for this SKU via the CoA/Spec Sheet.

Quality and Grades

Item-specific grade/purity details: Not specified for this item; refer to CoA/Spec Sheet.

Context for enzyme product quality (general, not item-specific):

• Activity definition: Enzyme lots are commonly qualified by catalytic activity (e.g., units per mg or per vial) under a defined assay (substrate, pH, temperature, H2O2 concentration). Always confirm the exact activity definition on the CoA to ensure comparability with literature protocols.
• Purity metrics: May include SDS-PAGE purity, specific activity, residual host proteins, carbohydrate content (glycosylation), and heme content. Trace stabilizers (e.g., salts, sugars, polyols) can be present by design to enhance stability.
• Endotoxin/bioburden: For research enzymes, these are typically not controlled to biopharma-grade thresholds unless explicitly stated. Do not assume cell-culture suitability unless specified.
• UV background: If using in spectrophotometric assays (e.g., veratryl alcohol at 310 nm), low background absorbance of the formulation is desirable; HPLC-grade buffers/reagents can help.
• Batch-to-batch considerations: Isoform distribution and glycosylation microheterogeneity are common for fungal peroxidases and may modestly affect kinetics and stability.

What this means for this SKU:

• Without an explicit grade on the label, treat the product as research-use enzyme. Confirm unit definition, recommended assay, and any stabilizers via the item’s CoA/Spec Sheet before quantitative or comparative work.

Reaction and Applications

Applications below reflect general literature use of lignin peroxidase and are not item-specific claims.

• Oxidative depolymerization of lignin and lignin model compounds: Catalyzes one-electron abstraction from nonphenolic aromatics with very high redox potentials, enabling C–C and C–O bond cleavage in lignin structures (literature).
• Veratryl alcohol oxidation: A canonical assay substrate; LiP oxidizes veratryl alcohol to veratraldehyde in the presence of H2O2, monitored at 310 nm (literature). Veratryl alcohol can also act as a redox mediator for bulky substrates.
• Selective aromatic functionalization: Facilitates oxidation of polycyclic aromatics, anisyl derivatives, and certain heteroaromatics under mild, aqueous, acidic conditions.
• Environmental/bioprocess: Dye decolorization, PAH transformation, and pulp biobleaching as part of white-rot fungal enzyme systems.
• Polymer/materials: Surface modification of lignocellulosics and oxidative grafting onto lignin-rich fibers for adhesion/compatibilization.

Mechanistic notes (literature):

• Catalytic cycle proceeds via Compound I and Compound II (oxo–ferryl heme species) formed by H2O2 activation; long-range electron transfer from a surface tryptophan enables oxidation of bulky, high-potential substrates.
• Over-oxidation/inactivation: Excess H2O2 leads to heme degradation; controlled dosing is critical.

Practical tips:

• Maintain acidic pH and low, continuous peroxide supply (e.g., syringe pump or in situ generation).
• Include stabilizers (e.g., glycerol) and avoid metal chelators unless required by the system.
• Verify unit definition and calibrate against a known standard reaction before scale-up.

Reaction Conditions

Item-specific recommended conditions are not provided; consult the CoA/Spec Sheet. The following are literature-based general conditions for lignin peroxidase and are not specifications for this SKU.

Typical assay/oxidation setup (literature):

• Buffer: 25–100 mM sodium tartrate or citrate, pH 2.5–3.5.
• Temperature: 20–30°C (ambient). Avoid prolonged exposure above ~35–40°C to limit denaturation.
• Substrate: Veratryl alcohol (model substrate) at 1–5 mM; other aromatics as applicable.
• Initiator: H2O2 at 50–300 µM initial, then continuous/stepwise feed to maintain low steady-state concentrations.
• Enzyme loading: Titrate to achieve linear initial rates; report in activity units defined by your assay.
• Aeration: Ambient air is generally sufficient; gentle mixing provides adequate O2 and homogeneity.
• Time: Minutes to hours depending on substrate and dosing strategy; monitor by UV–vis (e.g., A310 for veratraldehyde) or HPLC.

Practical tips:

• Quench residual peroxide (e.g., with catalase or sodium thiosulfate) before analytical workup.
• Avoid metal chelators, strong surfactants, and high organic cosolvent fractions that can destabilize the enzyme.
• If substrates are poorly soluble, use minimal DMSO/EtOH cosolvent, cyclodextrins, or emulsions rather than large solvent volumes.

Expected outcomes: Selective oxidation to corresponding cation-radical–derived products; yields vary widely with substrate, mediator, and dosing protocol (literature).

Safety and Handling

Hazard information for this item:

• GHS classification, signal word, pictograms, and H-statements: Not specified for this item; refer to SDS.

General safety considerations for handling lignin peroxidase and related oxidative enzymes (literature/general guidance; not item-specific):

• Hazards: Enzyme powders and aerosols may cause respiratory or skin sensitization in susceptible individuals. The enzyme uses hydrogen peroxide (H2O2) as an oxidant; H2O2 is corrosive/oxidizing—manage separately according to its SDS.
• Incompatibilities: Avoid contact with strong oxidants beyond controlled assay conditions, strong acids/bases that denature proteins, and metal chelators that may disrupt heme environment.
• PPE: Lab coat, safety glasses, and appropriate gloves. Handle powders in a fume hood or biosafety cabinet to minimize aerosolization. Avoid inhalation and contact with skin/eyes.
• Handling: Keep on ice during use if supplied as an aqueous solution. Minimize freeze–thaw cycles. Prepare fresh H2O2 working solutions at low micromolar–millimolar levels as dictated by your assay to limit enzyme inactivation.
• First aid (overview; defer to SDS):
  • Inhalation: Move to fresh air; seek medical advice if symptoms persist.
  • Skin/eye contact: Rinse with water for at least 15 minutes; remove contaminated clothing; seek medical attention if irritation persists.
  • Ingestion: Rinse mouth; seek medical advice.

Always consult the product SDS for authoritative hazard, exposure controls, and spill/accident procedures.

Solvent Selection

This product is a protein enzyme and is typically used in aqueous buffer systems; classical “solvent selection” for small molecules is not directly applicable.

General/literature guidance for medium selection with lignin peroxidase (not item-specific):

• Primary medium: Aqueous buffers at acidic pH (often citrate, tartrate, or acetate) to support activity. Ionic strength and buffer species can influence stability and redox potential.
• Cosolvents: Low percentages of water-miscible organic cosolvents (e.g., glycerol for stabilization; small amounts of methanol/ethanol or DMSO to solubilize aromatic substrates) may be tolerated but can reduce activity at higher levels. Empirically titrate and keep total organic content as low as feasible.
• Peroxide delivery: Use freshly prepared, dilute H2O2 in buffer or generate in situ (e.g., via glucose oxidase) to mitigate enzyme inactivation from peroxide spikes.
• Oxygen: Reactions are typically conducted under ambient air; excessive deoxygenation is generally unnecessary.

When to choose alternatives:

• For neutral pH or manganese-dependent oxidations of phenolics, manganese peroxidase (MnP) or versatile peroxidase (VP) may be better suited (literature). Laccase can be preferred for O2-driven oxidations without added H2O2.

Practical tip:

• If substrate solubility is limiting, consider emulsions, cyclodextrin inclusion, or mediator systems rather than increasing organic cosolvent beyond enzyme tolerance.

Storage and Reconstitution

Storage conditions (item-specific):

• Store at -20°C.
• Shipped in: Ice chest + ice pads.

Additional notes:

• Avoid repeated freeze–thaw cycles; aliquot upon first use if supplied as a solution.
• Protect from contamination; use clean, enzyme-compatible plasticware/glassware.

Reconstitution details: Not specified for this item; refer to CoA/Spec Sheet.

General handling guidance (literature; not item-specific): If supplied lyophilized, many peroxidases reconstitute in cold, acidic buffer (e.g., 25–50 mM tartrate or citrate, pH ~3–4) with gentle mixing. Inclusion of 10–20% glycerol can enhance stability for refrigerated storage. Verify compatibility with your downstream assay before adopting any stabilizers.

Structure and Identity

Item-specific identifiers: not specified for this item; refer to CoA/Spec Sheet.

• CAS: 93792-13-3
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• SMILES / InChI / InChIKey: Not specified for this item; refer to CoA/Spec Sheet.

General/literature description (not item-specific):

• Lignin peroxidase (LiP; EC 1.11.1.14) is a heme-containing oxidoreductase enzyme produced by certain white-rot fungi. It catalyzes one-electron oxidations of high-redox-potential aromatic substrates using hydrogen peroxide as the terminal oxidant.
• Structural features (typical, literature):
  • Single polypeptide, glycosylated, incorporating a protoporphyrin IX heme cofactor ligated by a conserved proximal histidine.
  • Typically contains disulfide bonds that stabilize the tertiary structure and an exposed tryptophan (e.g., Trp171 in some isoforms) involved in long-range electron transfer to bulky aromatics (literature).
  • Predominantly α-helical fold characteristic of class II fungal peroxidases.
• 2D “structure in words”: A globular protein with a buried iron–protoporphyrin active site and surface-accessible substrate interaction patches; no small-molecule SMILES applies since this is a proteinaceous enzyme preparation.

Important note:

• Exact isoform, sequence, glycoform distribution, and activity units for this catalog item are not specified; consult the product CoA/Spec Sheet for item-specific identity confirmation (e.g., source organism, activity definition, and assay conditions).

Synthetic Utility

General/literature perspectives on synthetic utility (not item-specific):

• Mild, selective oxidations: Enables one-electron oxidations of challenging, high-redox-potential aromatics in water at ambient temperature, often complementing or replacing harsh chemical oxidants.
• C–C/C–O bond cleavage in lignin motifs: Facilitates depolymerization of lignin model dimers, generating monomeric aromatics amenable to downstream functionalization.
• Mediated transformations: Veratryl alcohol and other mediators can shuttle electrons, expanding substrate scope to bulky or poorly soluble aromatics.
• Late-stage modification: Site-selective oxidation of complex aromatic scaffolds under biocompatible conditions can open routes to novel derivatives.
• Materials chemistry: Oxidative coupling/grafting on lignocellulosic surfaces; valorization of lignin to functional materials.

Strategic considerations:

• Choose LiP when substrate oxidation potential exceeds the reach of laccase or MnP; verify by cyclic voltammetry or literature precedent.
• Implement controlled H2O2 feed; consider in situ generation to balance rate and stability.
• Immobilization (on resins, nanoparticles, or within polymers) can enhance operational stability and reusability, albeit with potential mass-transfer limitations.

Note: Exact activity units, turnover numbers, and kinetic parameters for this SKU are not specified and must be obtained from the CoA or determined empirically under your conditions.

Target Specificity

Not applicable to this product type. Target specificity, clone, isotype, and species reactivity apply to antibodies or affinity reagents, not to enzyme preparations. For functional selectivity of lignin peroxidase, see Reaction & Applications and Synthetic Utility.