Catalase, CAS No.9001-05-2

CAS: 9001-05-2 Cat. No.: C757781 Número CE: 232-577-1

GRAU & PUREZA EnzymoPure™, ≥25000 CIU/g

Especificações

Product Name

Catalase, CAS No.9001-05-2

Grau

EnzymoPure™

Especificações e pureza

EnzymoPure™, ≥25000 CIU/g

CAS

9001-05-2

Número da Comissão das Enzimas

E.C.1.11.1.6.

Tipo de molécula

Enzyme

Armazenamento e envio

Concentração

≥25000 CIU/g

Condições de armazenamento de armazenamento

Store at 2-8°C,Protected from light

Enviado em

Wet ice

Definição da unidade

The activity is determined relative to an enzyme standard. The result is given in the units CIU/g.

Application Protocols

Tested, item-specific application protocols (e.g., validated assay conditions, recommended working concentrations, or specific workflows) are not provided in the Product Data.

• Item-specific recommended uses and dilutions: Not specified for this item; refer to CoA/Spec Sheet.

General guidance is provided under the “Reaction Conditions” tab for literature-based catalase assays; however, these are not validated protocols for this specific product lot.

Biological Roles

Catalase is a ubiquitous peroxisomal/ bacterial enzyme central to cellular oxidative stress management (general, literature).

• Function: Rapidly decomposes H2O2, a reactive oxygen species formed by oxidases and during aerobic metabolism, to prevent damage to proteins, lipids, and nucleic acids.
• Localization: In eukaryotes, predominantly peroxisomal; in many bacteria/archaea, cytosolic or periplasmic. Some isoenzymes are secreted or associated with membranes.
• Cofactor: Heme b (protoporphyrin IX–Fe); some catalases bind NADPH to mitigate compound I–mediated inactivation.
• Kinetics: Exhibits extremely high turnover numbers with H2O2 as both oxidant and reductant; classical ping-pong mechanism via ferryl porphyrin cation radical intermediates (Compound I/II).
• Physiological integration: Works in concert with peroxidases and superoxide dismutases—SOD converts superoxide to H2O2, which is then disproportionated by catalase.
• Genetic/isoform diversity: Multiple catalase families (mono-functional heme catalases; catalase–peroxidases) with differing pH optima and inhibitor profiles across species.

Notes for researchers:

• Source-specific behavior matters—pH/activity profiles and inhibitor sensitivities vary. If biological mimicry is important (e.g., peroxisomal conditions), match ionic strength and pH to the native environment.
• No medical or clinical claims are made for this product. It is supplied strictly for research use.

Buffer Applications

Catalase is not used as a buffering reagent. However, successful use of catalase depends critically on suitable buffer conditions. The following guidance is general/literature-based.

• pH range: Near-neutral pH (≈6.8–7.5) typically supports high activity and stability; verify with your specific preparation.
• Common buffers: 50 mM potassium phosphate (pH 7.0) or 50 mM Tris-HCl (pH 7.5). For UV assays at 240 nm, phosphate is advantageous due to low absorbance.
• Ionic strength: 50–200 mM salt (KCl/NaCl) can stabilize protein structure; optimize empirically.
• Stabilizers (storage): 10–50% v/v glycerol, 0.1–1% w/v trehalose/sucrose, and 0.1–1 mg/mL carrier protein (e.g., BSA) are commonly used to improve shelf-life; compatibility depends on downstream readouts.
• Metal ions: Trace metals can catalyze non-enzymatic H2O2 decomposition; low levels of EDTA (e.g., 0.1–1 mM) may help, provided it does not disrupt other components.
• Inhibitors to avoid: Sodium azide and cyanide strongly inhibit heme enzymes, including catalase; do not include if activity is required.

Example assay buffer (literature, illustrative): 50 mM potassium phosphate, pH 7.0, 25 °C. Initiate reaction by adding H2O2 to the desired concentration and follow A240 decay. This is guidance only and not an item-specific specification.

Green Alternatives

Catalase itself embodies green chemistry principles by catalyzing the benign conversion of hydrogen peroxide into water and oxygen, reducing the need for stoichiometric quenchers or metal catalysts.

Comparison of peroxide-removal strategies (general, literature):

• Approach: Catalase (biocatalyst) • Advantages: High selectivity for H2O2; water/O2 as products; effective at ambient conditions; minimal waste. • Trade-offs: Sensitive to inhibitors and denaturation; requires aqueous conditions and appropriate pH; activity depends on formulation.

• Approach: Chemical reductants (e.g., sodium bisulfite, thiosulfate) • Advantages: Robust, shelf-stable, inexpensive. • Trade-offs: Introduce salts/sulfur residues; pH shifts; potential interferences with analytics and downstream enzymes.

• Approach: Heterogeneous scavengers (e.g., MnO2) • Advantages: Simple solid–liquid operations; heat generation can be useful. • Trade-offs: Introduces solids/particulates and metal residues; less selective; can over-oxidize sensitive components.

Guidance for greener workflows:

• Use catalytic amounts of catalase under mild, aqueous, near-neutral conditions; minimize added salts and avoid azide preservatives when activity is required.
• Combine with glucose oxidase to establish controlled low-peroxide, low-oxygen environments without harsh chemicals.
• Validate that buffer components are benign and readily treatable in wastewater (e.g., phosphate or Good’s buffers) and avoid volatile organic solvents.

Item-specific environmental certifications or green metrics: Not specified for this item; refer to CoA/Spec Sheet.

Pharmaceutical Uses

No therapeutic or clinical claims are made for this material. For research and process development only.

General, non-clinical roles in pharmaceutical/bioprocess settings (literature/practice):

• Processing aid for peroxide removal: Decomposes residual H2O2 after aseptic filtration, viral inactivation, or peroxide-based sanitization, minimizing chemical impurities before sensitive steps.
• Analytical/QA support: Serves as a control reagent for validating peroxide-specific assays or demonstrating specificity of oxidative stress tests in formulation studies.
• Enabling enzyme cascades: Protects peroxide-sensitive biocatalysts during oxidase- or aeration-coupled transformations in process development.
• Device and material compatibility studies: Used to quench surface or packaging peroxide residues during extractables/leachables or stability evaluations.

Regulatory and compendial status:

• Pharmacopeial monographs or excipient listings for this specific product/lot are Not specified for this item; refer to CoA/Spec Sheet and applicable regulations if considering use beyond basic research.

Formulation cautions:

• Preservatives such as sodium azide are incompatible with catalase activity; verify formulation components on the Spec Sheet before incorporating into assays or process streams.

Physical Properties

Item-specific physical constants are not provided for this enzyme preparation. The following notes distinguish catalog specifications from general literature properties.

Item-specific (catalog):

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• Solubility: Not specified for this item; refer to CoA/Spec Sheet.

General/literature properties (for catalase proteins):

• Aggregation state: water-soluble globular protein; readily soluble in neutral to mildly basic aqueous buffers with moderate ionic strength; precipitates in strong organic solvents or at extremes of pH.
• Thermal behavior: denaturation typically observed above ~50–60 °C depending on buffer, ionic strength, and stabilizers (literature). Boiling irreversibly inactivates the enzyme.
• Isoelectric point (pI): varies by species/isoform; commonly in the acidic range (~pI 5–6, literature).
• Spectroscopy: strong Soret band near ~405 nm due to heme; H2O2 turnover can be followed by the decrease in A240 (H2O2 absorbance) or O2 evolution (literature).
• Activity units: commonly reported as units per mg, where 1 unit decomposes 1 µmol H2O2 per minute at defined conditions (e.g., 25 °C, pH ~7.0, specified H2O2 concentration; literature). These are not item specifications.

Unavailable properties for macromolecules:

• Boiling point, melting point, density, logP, refractive index: not meaningful for proteins in the dry sense; behavior depends on formulation and hydration state.

Quality and Grades

• Grade/Purity: EnzymoPure™ (item-specific).

What EnzymoPure™ typically implies (general description):

• Designed for research-grade enzymology and biochemistry where high specific activity and low contaminant background are important. Emphasis is commonly placed on minimal nuclease/protease contamination, controlled stabilizers, and batch-to-batch consistency. Exact acceptance criteria (e.g., activity units/mg, residual DNase/RNase, protease activity, endotoxin) are Not specified for this item; refer to CoA/Spec Sheet.

Considerations for enzyme quality:

• Specific activity: Primary performance indicator for catalase preparations. Verify units/mg and assay conditions on the CoA; activity depends strongly on buffer composition and assay pH/temperature.
• Purity and homogeneity: SDS-PAGE or SEC-HPLC profiles are often used to assess subunit purity and aggregation; details Not specified for this item.
• Stabilizers: Proteins may be formulated with glycerol, sugars, or salts to enhance stability. Presence/absence and concentrations are Not specified for this item; refer to CoA.
• Bioburden/endotoxin: Relevant for sensitive cell-free or diagnostic workflows. Not specified for this item.

Practical guidance:

• Match the assay conditions on your CoA when benchmarking activity.
• If low-UV background is critical (e.g., following H2O2 at 240 nm), ensure the formulation lacks UV-absorbing excipients—verify on the Spec Sheet.
• Record lot number and retain CoA for method validation and regulatory documentation.

Reaction and Applications

Catalase catalyzes 2 H2O2 → 2 H2O + O2 with exceptionally high turnover (literature). This makes it valuable as a benign H2O2 scavenger and oxygen generator in research workflows.

Representative applications (research use only):

• H2O2 removal in oxidase-coupled assays: Protects sensitive enzymes (e.g., dehydrogenases, monooxygenases) from oxidative inactivation by degrading byproduct H2O2 while allowing analytical readouts to proceed.
• Quenching residual peroxide: After peroxidase reactions or sterilization with H2O2, catalase can be used to rapidly eliminate leftover peroxide prior to downstream steps that are peroxide-sensitive.
• Oxygen management: Generates O2 in situ for microaerobic/aerobic biotransformations or for calibration of oxygen sensors; conversely, in combination with glucose oxidase, catalase helps maintain low steady-state H2O2 and can modulate dissolved O2.
• Surface/gel treatments: Deperoxidation of polymer surfaces or gels that were pretreated with peroxide initiators (research and materials labs).
• Analytical assays: Kinetic monitoring of peroxide decay at 240 nm or via O2 electrodes/manometry; serves as a standard enzyme in teaching and method development (literature).

Practical notes:

• Avoid inhibitors (azide, cyanide, heavy metals). Chelators (EDTA) may help mitigate metal-catalyzed peroxide decomposition but should not compromise enzyme structure.
• Control H2O2 levels—excess peroxide can inactivate catalase. Add substrate incrementally or operate under steady-state conditions.
• Maintain near-neutral pH and moderate ionic strength; keep solutions cold when not reacting; protect from light to preserve the heme.

Reaction Conditions

The following are general, literature-based conditions for catalase assays and process use. They are not specifications for this item.

Typical assay conditions (spectrophotometric):

• Buffer: 50 mM potassium phosphate, pH 7.0.
• Temperature: 20–25 °C (control precisely for kinetic work).
• Substrate: H2O2 prepared fresh; initial concentrations commonly 5–50 mM for rapid assays—optimize to avoid enzyme inactivation.
• Readout: Monitor decrease in A240 (ε240 for H2O2 ≈ 43.6 M−1 cm−1, literature) or measure O2 evolution with a Clark electrode/manometry.
• Enzyme dosing: Adjust to achieve linear initial rates; start in the low nM–µM active-site range depending on activity units provided on the CoA.

Process/application notes:

• pH range: Neutral to mildly basic (≈6.8–8.0) typically maintains activity; confirm for source-specific variants.
• Ionic strength: Moderate salt (50–200 mM) often stabilizes structure; avoid extremes.
• Inhibitors: Avoid sodium azide, cyanide, and high concentrations of heavy metals; chelators (e.g., 0.1–1 mM EDTA) may be beneficial against adventitious metals.
• Light: Protect from strong light to preserve the heme; follow the item’s storage note to protect from light.
• Substrate feed: For quenching applications, add catalase first, then titrate H2O2; excess peroxide can lead to transient inactivation and heat generation.

Expected performance: High apparent kcat enables rapid peroxide clearance; actual rates depend on formulation and specific activity (verify on CoA/Spec Sheet).

Safety and Handling

GHS/SDS classification for this specific item is not provided here. Always consult the product SDS for authoritative safety information.

Item-specific hazard details:

• Signal Word: Not specified for this item; refer to SDS.
• H-Statements/GHS Classification/Pictograms: Not specified for this item; refer to SDS.

General laboratory safety for protein enzymes:

• Hazards: While catalase is not typically hazardous, proteins can be allergenic upon repeated exposure. Avoid inhalation of aerosols and contact with eyes and skin. Solutions may contain buffers/preservatives—review SDS.
• PPE: Use lab coat, safety glasses, and suitable gloves. Work in a clean area to avoid microbial contamination of the enzyme.
• Handling: Keep cold (2–8 °C as specified for this item) and protect from light to preserve the heme cofactor. Avoid vigorous vortexing or foaming that can denature proteins.
• Incompatibilities (general, literature): strong oxidants beyond substrate levels, heavy metal ions, azide and cyanide (heme enzyme inhibitors), extremes of pH, and organic solvents that disrupt protein structure.
• First aid (general): In case of contact, rinse affected area with water. If inhaled, move to fresh air. If ingested, rinse mouth with water. Seek medical attention if symptoms persist. Follow institutional protocols.
• Spills and disposal: Absorb aqueous spills with inert material; clean with water/detergent. Dispose according to local regulations for nonhazardous biological laboratory waste unless SDS indicates otherwise.

Solvent Selection

Catalase is an aqueous, proteinaceous biocatalyst; solvent selection centers on buffer systems rather than organic solvents.

• Polarity class: Hydrophilic macromolecule; functions in water-based buffers. Insoluble/denatured in most neat organic solvents.
• Miscibility profile: Use fully aqueous buffers (e.g., phosphate, Tris, HEPES). Limited tolerance to cosolvents (often ≤10% v/v glycerol or ≤5% v/v low-chain alcohols) depends on formulation; verify experimentally. Avoid strong denaturants (urea, guanidinium) unless intentionally unfolding.
• Dielectric constant/logP: Not applicable to proteins in the conventional sense.

Choosing buffers (general, literature):

• pH window: Catalase activity is typically highest near neutral pH (≈6.8–7.5) but can vary by source. Maintain ionic strength (50–200 mM) to support structural stability.
• Stabilizers: Glycerol (10–50% v/v for storage), sugars (trehalose/sucrose), and mild salts can improve stability. Sodium azide inhibits heme enzymes; avoid if catalytic activity is required.

Comparison (general):

• Phosphate vs Tris: Phosphate offers strong buffering at pH ~7 and is UV-transparent at 240 nm (for H2O2 assays); Tris has higher temperature sensitivity of pKa.
• HEPES/Good’s buffers: Excellent biological compatibility and minimal metal binding; suitable for kinetic studies.

Tip: If coupling catalase with other enzymes (oxidases/peroxidases), select a buffer compatible with all catalysts and avoid chelators or inhibitors that could interact with the heme or partner enzymes.

Storage and Reconstitution

Item-specific storage/shipping (from Product Data):

• Storage Conditions: Store at 2–8 °C, protected from light.
• Shipped In: Wet ice.

Additional, general guidance (literature/best practice; not item-specific specifications):

• Short-term handling: Keep on ice during use. Minimize time at room temperature. Avoid repeated freeze–thaw cycles; if freezing is necessary and compatible with the formulation, aliquot with 10–50% v/v glycerol and store at ≤−20 °C. Confirm compatibility on the Spec Sheet.
• Reconstitution (if supplied lyophilized; status Not specified for this item): Reconstitute with cold, oxygenated buffer such as 50 mM potassium phosphate, pH ~7.0. Allow gentle mixing without foaming. Let the vial equilibrate to 2–8 °C before opening to avoid condensation.
• Working solutions: Prepare in buffer free of azide/cyanide and heavy metals to maintain activity. Filter sterilize (0.22 µm) only if necessary and if activity retention is confirmed.
• Light protection: Use amber tubes or wrap containers in foil to protect the heme cofactor from photodegradation, consistent with the product’s “protect from light” note.
• Stability: Exact shelf-life and specific activity retention over time are Not specified for this item; refer to CoA/Spec Sheet. Monitor enzyme performance periodically using a standard H2O2 assay to verify activity.

For research use only.

Structure and Identity

Catalase (EC 1.11.1.6) is a heme-dependent oxidoreductase that disproportionates hydrogen peroxide to water and dioxygen.

• SKU: C757781
• Product Name: Catalase
• CAS: 9001-05-2
• PubChem CID: 8434 (protein entry)
• Molecular Formula (item-specific): Not specified for this item; refer to CoA/Spec Sheet.
• Molecular Weight (item-specific): Not specified for this item; refer to CoA/Spec Sheet.
• InChIKey: Not specified for this item; refer to CoA/Spec Sheet. (Note: proteins typically do not have InChIKeys.)
• SMILES: Not specified for this item; refer to CoA/Spec Sheet. (Note: not generally used for macromolecular enzymes.)

Structural features (general, literature):

• Quaternary structure: usually a homotetramer of ~60 kDa subunits (literature), each harboring one protoporphyrin IX (heme b) cofactor and a deeply buried active site channel.
• Active site: conserved distal His/Tyr pair and essential heme iron; some catalases contain an NADPH-binding pocket that mitigates oxidative inactivation (literature).
• 2D description in words: a globular protein composed of α/β domains; each subunit contains a porphyrin macrocycle (heme) coordinated to Fe and embedded within a protein pocket accessible via a narrow channel for H2O2 diffusion.

Notes:

• Source organism, exact subunit mass, glycosylation state, and sequence are item-specific quality attributes and are Not specified for this item; refer to CoA/Spec Sheet.

Synthetic Utility

Catalase is a valuable auxiliary biocatalyst in chemoenzymatic synthesis and analytical chemistry (general, literature).

Key roles:

• Peroxide management in oxidase-coupled systems: Glucose oxidase, alcohol oxidase, and amino acid oxidase generate H2O2; catalase prevents side-oxidations and extends lifetime of partner enzymes.
• Driving equilibria and selectivity: By removing H2O2, catalase can shift reaction networks away from undesired peroxidations, improving selectivity in oxidation cascades.
• Oxygen supply modulation: Controlled O2 generation from H2O2 can be harnessed for oxygen-sensitive steps at small scale, aiding microreactor and sensor development.
• Materials and polymer chemistry: Post-polymerization quench of peroxide initiators to stop radical processes without introducing reducing agents that may contaminate products.

Mechanistic considerations:

• Ping-pong mechanism via ferryl heme intermediates (Compound I/II); extremely high kcat necessitates careful substrate dosing to avoid self-inactivation by excess H2O2 (literature).
• Inhibitors: Azide, cyanide, and heavy metals bind heme, reducing turnover; avoid in reaction mixtures.

Operational guidance:

• Run at near-neutral pH in phosphate or Good’s buffers; maintain temperature in the 20–30 °C range unless otherwise validated.
• Introduce H2O2 gradually (syringe pump or fed-batch) to keep concentrations modest; this preserves activity and smooths O2 evolution.
• If UV monitoring at 240 nm is used, verify that other components do not absorb significantly at this wavelength.

Target Specificity

This section is typically applicable to antibodies or affinity reagents. Catalase is an enzyme, not an affinity reagent.

• Tested targets/epitopes, clone IDs, isotypes, or species reactivity: Not applicable to this product.
• Item-specific target-binding data: Not specified for this item; refer to CoA/Spec Sheet if any affinity tags or fusions are present (not indicated here).

Perguntas frequentes

How should this product be stored?

Store at 2–8 °C, protected from light. The material is light-sensitive — keep it in its original opaque or amber container.

What is EnzymoPure??

EnzymoPure? is one of Aladdin Scientific's premium product lines, formulated for high-purity applications across multiple workflows. Compared to standard grades in the same workflow, EnzymoPure? products typically offer tighter specifications, more rigorous QC, and stronger lot-to-lot consistency.

How is this product shipped?

This product ships chilled on wet ice. Unpack on arrival and transfer it to the storage condition stated above.

What are the CAS number, molecular formula and molecular weight?

The CAS Number is 9001-05-2.

What documentation is provided?

Available product documentation, including Certificates of Analysis (COA), Safety Data Sheets (SDS), and specification sheets, is shown in the product document area. Document availability and access follow the current site policy.