| HS Code | 422178 |
| Productname | Catalase |
| Casnumber | 9001-05-2 |
| Ecnumber | 1.11.1.6 |
| Enzymeclass | Oxidoreductase |
| Systematicname | Hydrogen-peroxide:hydrogen-peroxide oxidoreductase |
| Molecularweight | Approximately 240 kDa (tetramer) |
| Optimumph | 7.0 |
| Optimumtemperature | 37°C |
| Substrate | Hydrogen peroxide (H2O2) |
| Reactionproducts | Water (H2O) and oxygen (O2) |
| Cofactor | Heme (iron protoporphyrin IX) |
| Source | Bovine liver (common); also microbial (Aspergillus niger) |
| Appearance | Brownish crystalline powder or suspension |
| Solubility | Soluble in water; practically insoluble in organic solvents |
| Storageconditions | Store at 2-8°C, protected from moisture |
| Biologicalfunction | Decomposes toxic hydrogen peroxide to water and oxygen |
As an accredited Catalase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Catalase, 10 g, supplied in a sealed amber glass bottle with tamper-evident cap and safety label. |
| Container Loading (20′ FCL) | Catalase 20′ FCL: packed in sealed drums/pails, palletized, secured, labeled, with ventilation to prevent moisture and degradation. |
| Shipping | Catalase shipments require cold-chain handling to preserve enzyme activity. Transport in insulated containers with wet ice, dry ice, or gel packs, typically at 2–8°C. Use leak-proof, sealed packaging with absorbent material, and clearly label as Biological Substance, Category B. Avoid shaking, extreme temperatures, and delays. Include safety data sheet and proper documentation. |
| Storage | Catalase should be stored as a lyophilized powder at 2–8°C in a tightly sealed, light-resistant container. Once dissolved, use immediately or store briefly at 2–8°C; avoid repeated freeze-thaw cycles, which reduce enzyme activity. Keep desiccated and away from reactive chemicals to maintain stability. |
| Shelf Life | Catalase should be stored at 2–8°C, protected from light; its typical shelf life is 12 months from manufacture. |
Across continuous knit finishing lines processing cotton and cotton/elastane single jersey between 160 and 240 g/m², residual hydrogen peroxide carried over from pad-batch bleaching ranges from 10 mg/L to 80 mg/L in the treatment bath after a single cold rinse. Residual oxidant at these concentrations cleaves vinyl sulfone and monochlorotriazine reactive dyes during subsequent exhaust dyeing, producing shade dulling, poor reproducibility, and unlevel dye uptake. Formulations containing catalase from Aspergillus niger with a declared activity of 50,000 U/mL are metered into the exhaust bath at 0.15–0.40 g/L after the residual peroxide has been measured by titanium sulfate photometric determination or equivalent peroxide test strips. The treatment is held at 30–50°C for 10–20 min at pH 6.5–9.0, with the enzyme decomposing hydrogen peroxide to water and molecular oxygen. The reaction follows first-order behaviour at low substrate concentration, and process control must account for the sharp loss of activity below pH 5.0 and above 55°C; therefore bath temperature is verified by a machine RTD probe rather than by panel display. Textile auxiliaries supplied to this segment are screened under OEKO-TEX ECO PASSPORT, and fabric dyed after catalase treatment is tested to ISO 105-C06:2010 and ISO 105-B02:2014 to confirm that peroxide residues have not compromised wash fastness or light fastness. Downstream production equipment typically includes soft-flow and air-jet dyeing machines with liquor ratios from 1:8 to 1:12, where batch-to-batch variation in residual peroxide is the primary processing bottleneck. Terminal finished goods produced through this route include cellulosic jersey, piqué knit, interlock, French terry, and woven cotton shirting, with catalase positioned after bleaching and before reactive dyeing rather than after dyeing.
| Control variable | Analytical method | Observed range in soft-flow knit bleaching | Catalase response |
|---|---|---|---|
| Residual H₂O₂ | Titanium sulfate photometric | 10–80 mg/L | 0.15–0.40 g/L dose at 50,000 U/mL |
| Bath pH | pH electrode | 6.5–9.0 | Optimal reaction; below 5.0 inactivation risk rises |
| Bath temperature | Machine RTD probe | 30–50°C | Above 55°C denaturation occurs |
| Reaction time | PLC cycle timer | 10–20 min | Residual H₂O₂ below 1 mg/L before dye addition |
In aseptic carton and pouch filling lines, hydrogen peroxide at 30–35% w/v is applied as a vapour or spray sterilant to polyethylene and paperboard contact surfaces; after hot-air removal, residual concentrations can remain above 0.5 mg/kg and must be eliminated before product contact. Catalase derived from Micrococcus lysodeikticus is listed for food-processing use under FDA 21 CFR 173.135 and is evaluated within the EU under food enzyme Regulation (EC) No 1332/2008; when used as a processing aid on food-contact surfaces, packaging compliance is assessed under EU Regulation (EC) No 10/2011. A dilute neutralising solution is prepared at 0.01–0.05 g/L catalase in potable water and applied by misting or rinsing after the drying section, at a surface temperature below 55°C to prevent heat denaturation. The reaction generates only water and oxygen, leaving no oxidant residue of toxicological concern, but released oxygen can create foam in narrow filler rinse channels. Production-scale obstacles include foam entrainment in the filler bowl, incomplete rinse coverage on pleated package geometry, and catalase carryover into the product if rinse flow is not validated before line start-up. Food packaging auditors verify residual peroxide on surfaces with EM Quant 10011 or equivalent semi-quantitative strips, and line operators monitor package rinse water conductivity to confirm removal of neutraliser solution. Terminal finished product types include UHT milk, fruit juice, liquid egg, and plant-based beverage cartons, as well as thermoformed cups and flexible pouch packaging produced in extended-shelf-life filling halls.
Downstream of advanced oxidation process reactors used to destroy recalcitrant textile dyes and chemical oxygen demand in industrial effluent, residual hydrogen peroxide entering the biological stage suppresses nitrifying bacteria and can trigger activated sludge bulking. Effluent treatment systems discharging to public sewers under permits referencing EU Industrial Emissions Directive 2010/75/EU BAT conclusions require peroxide neutralisation before microorganism contact, with residual H₂O₂ measured by ASTM D6994-15 or equivalent periodic titrimetric verification. Catalase is dosed at 0.05–0.20 g/L of a 50,000 U/mL preparation per cubic metre of effluent when inlet peroxide residual is 10–25 mg/L. The neutralisation step is carried out in a baffled tank with a hydraulic residence time of 30–45 min, using a submersible mixer and a Pt-Ag/AgCl oxidation-reduction potential probe to confirm peroxide decay. The enzyme is heat-labile above 45°C and is inhibited by free copper, iron, and mercury above 1 mg/L in alkaline AOP side streams; therefore the feed is cooled and filtered if upstream Fenton chemistry carries over dissolved metal ions. Terminal finished product type is not a consumer article but a compliant industrial wastewater stream suitable for sewer discharge or partial reuse in pre-washing and screen washing, with the biological treatment stage protected from oxidative inhibition.
In preservative-free contact lens disinfection systems, the stored solution contains 3% w/v hydrogen peroxide in a low-ionic-strength formulation; exposure to catalase converts residual peroxide to saline and oxygen before the lenses are inserted. The relevant microbiological performance standard is ISO 14729:2017, which requires defined log reductions for bacteria and fungi through the soaking and neutralisation steps; lens packaging and labelling are additionally assessed under ISO 18369-1:2017. A neutralising tablet may contain catalase activity sufficient to decompose 3 mL of 3% H₂O₂ within 4–6 hours, with tablet dissolution controlled to avoid concentrated enzyme zones that would produce excessive froth in the lens case. Some liquid neutraliser architectures meter 0.5–1.0 mL of a buffered catalase solution into the case before lens insertion; final pH after neutralisation is maintained at 6.8–7.2 and osmolality at 280–320 mOsm/kg to match ocular surface tolerance. Production bottlenecks include shelf-life loss of catalase in solution through aggregation at 40°C and inhibition by heavy metals such as copper and iron, which complex the haem prosthetic group. Published data for this specific formulation configuration is limited, so accelerated stability tests at 25°C and 40°C over 90 days are used to validate activity retention. Terminal finished product types are single-use and repeat-use hydrogen peroxide lens care kits for soft silicone hydrogel and rigid gas permeable lenses.
When glucose oxidase is added to no-time dough formulations at 5–20 ppm enzyme protein for oxidative gluten strengthening, catalase co-formulated at 10–30% of glucose oxidase activity limits hydrogen peroxide accumulation in the dough matrix and prevents excessive stiffening of the gluten network. The enzyme preparation is assessed under food enzyme Regulation (EC) No 1332/2008, and catalase is specified in JECFA enzyme monographs; formulations intended for North American markets are aligned with FDA food-enzyme provisions for processing aids. In spiral mixers operating at high-speed intervals of 4–10 min and a final dough temperature of 26–28°C, the catalase addition corresponds to 2–15 ppm enzyme protein on flour weight. The controlled decomposition of peroxide to water and oxygen modulates sulfhydryl oxidation without eliminating the desirable dough-strengthening effect of glucose oxidase. Terminal finished product types include sandwich bread, hamburger buns, frozen dough pieces, and laminated pastry bases, with the catalase-containing enzyme blend added at the dry-ingredient stage rather than during late dough development.
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Catalase, EC 1.11.1.6, is a tetrameric heme-containing oxidoreductase that catalyses the disproportionation of hydrogen peroxide to water and molecular oxygen: 2 H2O2 → 2 H2O + O2. The enzyme has one of the highest known turnover numbers, with published values on the order of 106–107 s−1 per heme for eukaryotic catalases. Commercial preparations are standardised by activity rather than protein weight because the catalytic function is the specification that governs peroxide removal. Liquid products derived from Aspergillus niger submerged fermentation are the most common industrial form; solid and immobilised products are used where liquid metering is impractical or where soluble protein in the process stream must be avoided.
One unit of catalase is conventionally defined as the quantity of enzyme that decomposes 1 µmol of hydrogen peroxide per minute at pH 7.0 and 25 °C. The activity assay is usually an initial-rate measurement by UV absorbance at 240 nm using the molar absorption coefficient of hydrogen peroxide, 43.6 L mol−1 cm−1. No single ISO method is widely cited in industrial product data sheets; therefore, activity units are comparable between suppliers only when substrate concentration, buffer, temperature, and pH are identical. Supplier ordering codes commonly encode source organism, physical form, and nominal activity. A liquid grade at 50,000 U/mL may be identified as CAT-L50; a powder grade at 100,000 U/g may be identified as CAT-P100. The model system is supplier-specific and has no universal industry designation. Liquid formulations typically contain polyhydric alcohols and buffering salts; the full stabiliser and preservative profile must be checked against discharge permits or food-contact authorisations.
| Specification field | Liquid grade | Powder grade | Immobilised grade |
|---|---|---|---|
| Nominal activity | 50,000–250,000 U/mL | 10,000–100,000 U/g | 50–500 U/g wet |
| Source organism | Aspergillus niger | Aspergillus niger | Aspergillus niger |
| Appearance | amber liquid | off-white powder | hydrated beads |
| Storage temperature | 4–8 °C | 20–25 °C dry | 4–8 °C |
| pH operating range | 5.0–9.0 | 5.0–9.0 | 5.5–8.5 |
| Process temperature | 30–60 °C | 30–60 °C | 25–50 °C |
Values are representative ranges compiled from publicly available technical bulletins. Exact storage stability depends on the preservative system and water activity. Liquid products are more sensitive to freeze–thaw cycles than powder products. Freeze–thaw cycling of liquid catalase can cause precipitation of stabiliser salts and loss of activity; therefore, storage below 0 °C is not recommended unless the data sheet specifically permits it. Powdered catalase should be reconstituted in demineralised water at 20–30 °C with gentle agitation. High-shear mixing should be avoided because interfacial denaturation at air–liquid surfaces reduces activity without necessarily producing a visible precipitate.
Liquid grades are typically filtered through 0.2 µm membranes to reduce microbial load, but this does not guarantee sterility. Powder grades require dust control because airborne enzyme protein can cause respiratory sensitisation in workers; local exhaust ventilation and dust masks are standard handling controls. Immobilised grades must be kept hydrated; drying of the polymer bed can crack the bead matrix and release enzyme fragments into the downstream stream.
After alkaline hydrogen peroxide bleaching, cotton and its blends retain hydrogen peroxide in fibre capillary water and on the fabric surface. Residual peroxide at 10–20 mg/L in the dye bath is sufficient to oxidise reactive dyes, producing shade deviation and unlevel surface colour. Catalase is applied because it converts peroxide to oxygen and water without adding reducing salts. The reaction follows saturable kinetics; at low residual peroxide concentrations, the rate becomes first-order in substrate. The enzyme dose must therefore be calculated from the maximum residual peroxide measured at the final squeezer outlet, not from fabric weight alone. On a continuous open-width washing range processing fabric at 60–100 m/min, the liquid preparation is metered into the last wash box by a flow-proportional dosing pump. A control protocol includes an iodometric titration check according to AATCC TM102 at the dye bath inlet. If the titration value exceeds 5 mg/L, dyeing is delayed until the residual oxidizer is destroyed.
Process boundary conditions are more restrictive than those for sulfite reduction. The fungal enzyme has a practical pH window of 5.0–9.0; hot alkaline carryover from kier scouring at pH 10.5–12.0 can reduce activity by an order of magnitude within minutes. Neutralisation with a low-foaming acid buffer to pH 6.5–8.0 and cooling to 40–60 °C are therefore standard before catalase injection. Temperatures above 70 °C shorten the half-life of soluble preparations to minutes, while temperatures below 20 °C reduce the reaction rate to commercially unacceptable residence times. The oxygen released during decomposition can generate foam in high-turbulence jet dyeing machines with short liquor ratios of 1:5 to 1:8. Antifoam selection is constrained because silicone-based products are generally tolerated, but strong reducing agents, cationic surfactants, and aldehyde-based biocides can inhibit the enzyme. Production-scale experience in jet machines indicates that foam can be managed by splitting the catalase dose across two injection points and by maintaining back-pressure in the fabric circulation line.
Because residual peroxide in the fibre interior can bleed out after a clean bath titration, quality-control sampling includes a fabric extraction test. A woven cotton fabric sample is cut at the selvedge after the last wash box, extracted in deionised water at 25–50 °C for 10 min, and the extract is titrated or tested with a peroxide indicator strip. If the extract value exceeds the dyehouse specification, the catalase dose is increased or the residence time is extended before dyeing is released.
Catalase does not introduce reducing residues that interfere with subsequent reactive dyes. Sodium metabisulfite residues, if not rinsed completely, can react with vinyl sulfone or halogenated heterocyclic reactive groups, causing dye yield loss and uneven fixation. Catalase treatment leaves no reducing residual if the enzyme is inactivated by the subsequent hot rinse or diluted below the detection limit. However, residual protein from overdosing can cause turbidity in the dye bath; the standard corrective action is to use the minimum titrated dose and follow with a short overflow rinse.
Catalase differs from sodium metabisulfite and sodium bisulfite in by-product profile and salt burden. Chemical reduction of hydrogen peroxide with metabisulfite proceeds stoichiometrically and generates sulfate/sulfite salts that increase discharge conductivity and can contribute to fabric tendering if not rinsed. Catalase is catalytic; the enzyme is not consumed by the reaction, and the reaction products are oxygen and water. For a 2,000 L bath containing 100 mg/L residual hydrogen peroxide, the chemical route adds dissolved solids in direct proportion to the molar dose, whereas the enzymatic route adds only the formulation salts contained in the enzyme dose. The enzymatic process is slower than sulfite reduction at ambient temperature but eliminates sulfur dioxide off-gassing and reduces effluent salt. Catalase cannot be used directly in strongly alkaline peroxide bleaching baths; it must be applied after pH adjustment, whereas sulfite can function at pH values above 10. Published data for continuous high-speed bleaching lines with catalase reconstitution from solid preparations is limited, and validation on the specific machine is required before replacing a sulfite neutralisation step.
| Parameter | Catalase | Sodium metabisulfite reduction |
|---|---|---|
| Mechanism | Enzymatic disproportionation | Stoichiometric reduction |
| Dose basis | Activity units | Molar stoichiometry |
| Reaction products | O2, H2O | Sulfate salts, possible SO2 |
| pH operating range | 5.0–9.0 | broad; acidic pH releases SO2 |
| Temperature optimum | 40–60 °C | ambient–80 °C |
| Salt burden | low | high |
| Residual peroxide test | AATCC TM102 | AATCC TM102 |
In aseptic packaging and electronics water treatment, catalase is used to destroy hydrogen peroxide in recirculated water streams where residual oxidizer must be eliminated before discharge or downstream membrane treatment. The enzyme is injected into a holding tank with a residence time of 10–30 min; downstream reverse-osmosis membranes are protected from oxidative degradation. This application requires a low-salt destruction route because sulfite dosing would increase the total dissolved solids and risk membrane fouling. Catalase activity is attenuated by hypochlorite and peracetic acid; therefore, biocidal oxidizers must be neutralised or separated before the catalase injection point.
For polyamide thin-film composite reverse-osmosis membranes, feed-water peroxide limits are commonly below 0.1 mg/L to prevent oxidative degradation of the barrier layer. Catalase is used upstream of the membrane when the feed water contains hydrogen peroxide from aseptic packaging or sterilisation rinse. The enzyme does not remove other oxidizers; therefore, free chlorine must be reduced by activated carbon or bisulfite before catalase injection. For potable water treatment, catalase would be assessed under NSF/ANSI/CAN 60 for drinking water treatment chemicals; the enzyme formulation must not contribute regulated contaminants above the single-product allowable concentration.
Immobilised catalase preparations are supplied as enzyme covalently bound to epoxy-activated methacrylate or polystyrene-divinylbenzene beads. The packed-bed configuration permits continuous peroxide destruction in recirculated rinse water without introducing soluble protein into the process stream. The beads are loaded into a jacketed column with a bed height-to-diameter ratio of 2:1 to 4:1 and a superficial flow velocity of 2–10 m/h. The observed activity is lower than that of the soluble preparation because of internal mass-transfer resistance; therefore, column sizing requires a packed-bed residence time of 5–20 min for inlet peroxide concentrations below 50 mg/L. Pressure drop across the bed is typically 0.5–2.0 bar, depending on bead diameter and flow rate. The operational boundary is defined by bead fouling and mechanical attrition. Suspended solids, iron oxide deposits, and biofilm growth reduce the apparent activity by blocking the pore network; a prefilter of 5–10 µm is required. The immobilised form is not suitable for high-viscosity process streams or for streams containing strong chelating agents that can strip the enzyme cofactor or disrupt the protein structure. Published data for specific packed-bed configurations is limited; laboratory-scale column tests with the actual process water are necessary to determine the observed half-life and replacement interval.
Bovine liver catalase and fungal catalase differ in pH and thermal stability. Aspergillus niger catalase is the dominant industrial source because it can be produced by submerged fermentation and formulated with wider pH tolerance. Bovine liver catalase is regulated as a direct food substance under 21 CFR 184.1921, but it is not the typical choice for textile or wastewater use due to higher cost and animal-origin restrictions. Peroxidase-based products are not direct substitutes; peroxidases require hydrogen donors and generate different oxidation products. Catalase is specific for hydrogen peroxide and does not act on other peroxides such as peracetic acid or benzoyl peroxide at commercially relevant rates.
