Recombinant Protein Expression Services
Recombinant Catalase Expression
Recombinant catalase expression services for extremophile enzyme studies, oxidative-stress research, and diagnostic enzyme development —.
What Recombinant Catalase Expression Is
Catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide into water and oxygen, functioning as a natural antioxidant that protects cells against oxidative damage. Because the native enzyme is often extracted from animal or plant tissue, recombinant production in a microbial host offers a defined, animal- and plant-contamination-free route to the same catalytic function — an approach commonly used for research, clinical chemistry, and industrial enzyme supply.
Recombinant catalase expression means cloning or synthesizing the catalase coding sequence into an expression vector, transforming a suitable host such as a non-pathogenic strain of E. coli, inducing protein production, and then purifying and characterizing the recombinant enzyme. The result is a reproducible protein product whose sequence, activity, and stability can be documented rather than inferred from a tissue source.
This service is built for groups working on extremophile enzymes, oxidative-stress biology, and diagnostic or industrial enzyme applications. Projects typically begin with a defined catalase sequence or source organism and end with purified enzyme plus the activity and stability data needed to move into downstream studies.
Catalase Chemistry
Catalase catalyzes the transformation of hydrogen peroxide into water and oxygen, protecting cells from oxidative damage. This reaction is the basis for activity assays and for the enzyme's use as a natural antioxidant in research and industrial settings.
- H2O2 decomposition to water and oxygen
- Natural antioxidant and oxidative-stress defense role
- Activity measured by hydrogen peroxide decomposition
Non-Pathogenic Expression Hosts
Recombinant catalase is commonly produced in a non-pathogenic strain of E. coli, which supports fast and sustainable production and avoids animal- or plant-derived contamination. Alternative microbial hosts can be evaluated when a project's enzyme or application calls for them.
- E. coli as the standard expression host
- Microbial origin, free from animal or plant contamination
- Alternative hosts assessed case by case
Purified, Characterized Enzyme
The recombinant enzyme is purified, often by affinity chromatography, and can be supplied as a lyophilized powder for stable handling. Characterization covers activity and stability so that downstream users know what they are working with.
- Affinity chromatography purification
- Optional lyophilization to stable powder
- Activity and stability documentation
Where Recombinant Catalase Fits
Catalase sits at the center of oxidative-stress biology and is widely used wherever hydrogen peroxide must be controlled or measured. Recombinant production makes the enzyme's sequence and performance reproducible, which matters when catalase is used as a reagent, a reference standard, or a study subject in extremophile enzyme research.
The table below summarizes common application areas and what recombinant catalase typically contributes in each. Specific performance requirements — activity level, buffer, formulation, and stability targets — are defined per project during scoping.
| Application Area | Typical Use | What Recombinant Catalase Offers | Scoping Consideration |
|---|---|---|---|
| Extremophile enzyme research | Studying heat-stable or cold-adapted catalases from microbial sources | Defined sequence and reproducible production in a non-pathogenic host | Source organism and target stability range |
| Oxidative-stress studies | Modeling antioxidant defense and H2O2 clearance | Consistent activity units for controlled experiments | Required activity level and assay format |
| Diagnostic chemistry | Enzymatic removal or measurement of hydrogen peroxide | Animal- and plant-contamination-free enzyme supply | Purity and formulation requirements |
| Industrial enzyme applications | Textiles, waste treatment, cosmetics, and disinfectant uses | Recombinant production suitable for scale-up evaluation | Stability under process pH and temperature |
How a Project Runs
Each engagement follows a defined sequence from sequence to characterized enzyme. Steps below describe what happens and what is delivered; the exact depth of each step is set in the project scope.
Construct Design and Cloning
The catalase coding sequence is synthesized or cloned into an expression vector with an appropriate promoter and selection markers, with tags chosen to support downstream purification and detection.
Transformation and Expression
The construct is transformed into a non-pathogenic expression host such as E. coli, and protein production is induced under conditions selected for the target enzyme's solubility and yield.
Harvest and Lysis
Cells are harvested and lysed, and the soluble fraction is prepared for purification. Expression conditions may be adjusted if the target partitions differently than expected.
Purification
The recombinant catalase is purified, commonly by affinity chromatography, with purity assessed by SDS-PAGE and identity supported by Western blot where required.
What Can Be Customized
Catalase projects vary widely in source organism, required stability, and downstream format. The following elements are commonly adjusted during scoping so the delivered enzyme matches the intended study or application.
Customization is defined case by case in the project scope rather than through fixed packages.
Gene and Construct Options
The catalase coding sequence can be synthesized from a provided sequence or cloned from a source organism, with codon usage and tag placement adjusted to support expression and purification.
- Gene synthesis or cloning from source
- Promoter and selection marker selection
- Tag placement for purification and detection
Expression Host Selection
E. coli is the standard non-pathogenic host for recombinant catalase production. Where a target enzyme or application suggests a different microbial system, alternative hosts can be evaluated as part of scoping.
- Non-pathogenic E. coli as default host
- Alternative microbial hosts assessed case by case
- Induction conditions tuned per construct
Purification and Lyophilization
Purification strategy and final formulation are matched to the intended use, including buffer composition and the option to deliver the enzyme as a lyophilized powder for stable storage and handling.
- Affinity chromatography purification
- Buffer and formulation matched to application
- Lyophilized powder option for stability
Service Scope
Scope is defined per project after consultation. The table describes the parameters that are typically discussed and the range of options available; the final specification is recorded in the project scope of work.
Quantities, purity targets, and characterization depth are agreed before work begins so that deliverables match the intended downstream use.
| Parameter | Typical Project Scope | Options | Notes |
|---|---|---|---|
| Catalase source | Defined sequence or source organism provided by the client | Synthesis or cloning from source | Sequence confirmed before expression |
| Expression host | Non-pathogenic E. coli as standard | Alternative microbial hosts evaluated case by case | Host choice tied to target enzyme behavior |
| Expression format | Induced shake-flask or controlled culture | Conditions tuned for solubility and yield | Scale agreed in scope |
| Purification | Affinity chromatography as the common route | Additional polishing steps when required | Purity assessed by SDS-PAGE |
| Activity characterization | Hydrogen peroxide decomposition assay | Activity units reported per batch | Assay conditions documented |
| Stability testing | Assessment across selected temperature and pH conditions | Range defined by application | Supports formulation decisions |
| Final formulation | Liquid or lyophilized powder | Buffer and excipient selection as scoped | Lyophilization supports stable handling |
| Documentation | QC summary with purity, identity, and activity data | Additional data packages as scoped | Delivered with the enzyme batch |
Deliverables and Quality Control
Deliverables are agreed in the project scope and typically include purified recombinant catalase plus the analytical data needed to confirm identity, purity, and activity. Where lyophilization is selected, the enzyme is supplied as a stable powder.
Quality control combines standard protein analytics with enzyme-specific activity measurement so that each batch is documented against the agreed specification.
| Deliverable | Description | Method | Format |
|---|---|---|---|
| Purified recombinant catalase | Recombinant enzyme purified from the expression host | Affinity chromatography | Liquid or lyophilized powder |
| Purity assessment | Protein purity and apparent molecular weight | SDS-PAGE | Image and report |
| Identity confirmation | Detection of the target protein | Western blot where required | Report |
| Activity data | Hydrogen peroxide decomposition activity | Activity assay with reported units | Report |
| Stability data | Behavior across selected temperature and pH conditions | Stability testing as scoped | Report |
| QC summary | Consolidated batch documentation | Compiled from the above analyses | Delivered with the batch |
Why Teams Choose This Service
Recombinant production replaces the variability of tissue-derived catalase with a defined sequence and a documented batch record. For extremophile enzyme studies and oxidative-stress work, that reproducibility is often the difference between a usable reagent and an uncontrolled variable.
The service is structured around the specific catalase a project needs, not a single catalog enzyme, so host, construct, and characterization are aligned to the intended application.
Defined Sequence, Defined Batch
Because the enzyme is produced from a known construct in a non-pathogenic host, each batch can be traced to a sequence and documented against the same specification.
- Sequence-confirmed construct
- Batch-level QC documentation
- Consistent activity reporting
Free from Animal and Plant Sources
Microbial-origin recombinant production avoids animal- or plant-derived contamination, which is relevant for diagnostic and clinical chemistry applications where source material matters.
- Microbial origin
- No animal or plant tissue starting material
- Suitable for reagent applications
Scoped to the Target Enzyme
Construct, host, purification, and characterization are selected for the specific catalase and its intended use, including extremophile enzymes with unusual stability requirements.
- Construct and host matched to target
- Stability testing aligned to application
- Formulation options including lyophilization
Stability and Formulation Considerations
Catalase performance depends heavily on how the enzyme is handled after purification. Stability across temperature and pH ranges is commonly assessed during characterization so that formulation and storage recommendations reflect measured behavior rather than assumption.
Where a project requires a stable powder format, lyophilization is available as a final formulation step. The appropriate buffer system and excipients are selected during scoping based on the target enzyme and its intended application.
Applications and Downstream Use
Recombinant catalase supports research and clinical chemistry applications as well as industrial uses in textiles, waste treatment, cosmetics, and disinfectant formulations. In each setting, the enzyme's role is the same: controlled decomposition of hydrogen peroxide.
For extremophile enzyme studies, recombinant production makes it possible to work with catalases from unusual source organisms under defined conditions, and to compare their stability and activity against well-characterized references.
FAQ
Which expression host is used for recombinant catalase?
Recombinant catalase is commonly produced in a non-pathogenic strain of E. coli, which supports fast and sustainable production and avoids animal- or plant-derived contamination. Where a target enzyme or application suggests a different microbial system, alternative hosts can be evaluated during scoping.
Can you work from a catalase sequence rather than a provided sample?
Yes. Projects can start from a catalase coding sequence, which is synthesized or cloned into an expression vector with an appropriate promoter and selection markers. If you have a source organism rather than a sequence, that can also be discussed during scoping.
How is catalase activity measured?
Activity is measured through the enzyme's catalytic reaction — the decomposition of hydrogen peroxide into water and oxygen. Reported activity units and the assay conditions used are documented in the batch QC summary so results can be interpreted in context.
Is the enzyme supplied as a liquid or a powder?
Both formats can be discussed. Purified enzyme can be supplied in liquid form, or lyophilized to a stable powder where a dry format is preferred for storage and handling. The final formulation is agreed in the project scope.
What stability data is provided?
Stability testing can cover selected temperature and pH conditions relevant to your application, with results reported alongside purity and activity data. The specific conditions tested are defined during scoping so the characterization matches your downstream use.
How is the project scoped and supported?
Scope, construct design, host choice, purification strategy, and characterization depth are agreed before work begins. You receive a named scientific contact at project start, milestone review calls, and email response within one business day.
References
- Yang H, Zhang X, Ma Z, et al. [Expression, purification and characterization of catalase from Corynebacterium glutamicum]. Sheng wu gong cheng xue bao = Chinese journal of biotechnology. 2020;36(8):1568-1577. View on PubMed
- Parida S, Sahoo PK. Antioxidant Defence in Labeo rohita to Biotic and Abiotic Stress: Insight from mRNA Expression, Molecular Characterization and Recombinant Protein-Based ELISA of Catalase, Glutathione Peroxidase, CuZn Superoxide Dismutase, and Glutathione S-Transferase. Antioxidants (Basel, Switzerland). 2023;13(1). View on PubMed
- Kormanová Ľ, Rybecká S, Levarski Z, et al. Comparison of simple expression procedures in novel expression host Vibrio natriegens and established Escherichia coli system. Journal of biotechnology. 2020;321:57-67. View on PubMed
- Guo R, Ji S, Wang Z, et al. Trichoderma asperellum xylanases promote growth and induce resistance in poplar. Microbiological research. 2021;248:126767. View on PubMed
- He H, Zhang Y, Xu S, et al. Genetic transformation of GmFBX322 gene and salt tolerance physiology in soybean. PloS one. 2024;19(9):e0307706. View on PubMed
- Xie G, Huang Y, Hu D, et al. Potentiation of Catalase-Mediated Plant Thermotolerance by N-Terminal Attachment of Solubilizing/Thermostabilizing Fusion Partners. International journal of molecular sciences. 2024;25(22). View on PubMed
Start a Recombinant Catalase Project
Share your catalase sequence or source organism, intended application, and the activity and stability characteristics you need. We will define the construct, host, purification, and characterization plan with you before work begins.