Introduction

Whether in food processing, in vitro diagnostics, or textile bleaching, residual hydrogen peroxide has long been an “invisible killer” affecting product quality and efficiency. Catalase (CAT), as a highly efficient natural catalyst, is the key to solving this challenge. Today, Hzymes launches a new generation of recombinant catalase, redefining industry standards with ultra-high purity, superior enzymatic activity, and outstanding stability.

1. Introduction to Catalase

Catalase is composed of four identical subunits, each containing a heme (Fe³⁺-porphyrin) prosthetic group and an NADPH binding site (the latter prevents enzyme inactivation). Hydrogen peroxide enters the enzyme’s active site through a hydrophobic channel, where it is decomposed into oxygen (O₂) and water, which are released on the other side. The catalytic reaction is as follows:

Catalase exhibits extremely high catalytic efficiency. For example, one molecule of bovine liver catalase can decompose 40 to 60 million hydrogen peroxide molecules per second, making it one of the fastest enzymes known in nature. Its catalytic rate constant (kcat/km) is approximately 10⁷ M⁻¹s⁻¹, approaching the theoretical diffusion-controlled limit of enzymatic catalysis.

2. Applications of Catalase

1) The Golden Guardian of Skin: How Superoxide Dismutase and Catalase Enable Anti-Aging Miracles

If you follow skincare ingredients, you are no stranger to the “antioxidant duo” — superoxide dismutase (SOD) and catalase (CAT). SOD catalyzes the dismutation of superoxide anion radicals, generating hydrogen peroxide and oxygen. However, hydrogen peroxide itself is a reactive oxygen species, and excessive accumulation can cause oxidative stress damage to cells. At this stage, catalase plays a critical role by rapidly decomposing hydrogen peroxide into harmless water and oxygen, effectively blocking secondary oxidative damage. Together, SOD and CAT form a highly efficient, continuous antioxidant enzyme system within cells, significantly enhancing the body’s ability to scavenge free radicals.

When applied in skincare products, they serve as powerful biotech tools to protect against environmental damage and delay skin aging. Ultraviolet radiation generates large amounts of free radicals in the skin. Traditional sunscreens only block or absorb UV light, but cannot eliminate internal oxidative damage. By incorporating SOD or CAT into sunscreens, products can achieve dual protection — “external defense and internal repair.” With advances in biotechnology, recombinant SOD and CAT are gradually replacing animal-derived enzymes to reduce immunogenicity and enhance purity and activity.

2) The Deoxygenation Magician Behind Cheese: How Catalase Safeguards Food Safety

In cheese production, raw milk sterilization is a critical step. Traditional high-temperature sterilization can effectively kill harmful microorganisms, but also destroys beneficial lactic acid bacteria, which are essential for flavor development and maturation. Worse still, high temperatures damage natural enzyme systems in milk, lowering product quality.

To address this, food scientists introduced a gentle and effective sterilization method — hydrogen peroxide (H₂O₂) treatment. Adding 0.1%–0.25% hydrogen peroxide to raw milk at low temperature efficiently eliminates harmful microbes while preserving lactic acid bacteria and natural enzyme activity. However, residual hydrogen peroxide can compromise flavor and nutrition, and must be completely removed. Here catalase takes the stage — it rapidly decomposes hydrogen peroxide into harmless water and oxygen within seconds, without generating toxic byproducts.

The Food and Agriculture Organization (FAO) and the World Health Organization (WHO) have approved the use of immobilized catalase technology in dairy products and confirmed its safety for human health.

3) The Guardian of Precision Diagnostics: Catalase as the “Interference Cleaner”

Clinical creatinine testing faces a major challenge — interference from endogenous creatine can cause results to be falsely elevated by more than 30%! In enzymatic creatinine assays, creatinine hydrolyzes into creatine, but endogenous creatine in serum also enters the reaction system. Conventional creatinase-oxidase methods cannot distinguish between “newly generated creatine” and “endogenous creatine,” both of which are oxidized to produce H₂O₂ that participates in chromogenic reactions, leading to systematically inflated results.

By adding creatinase (CR) + sarcosine oxidase (SOX) + catalase (CAT) into reagent R1, an interference-clearing chain is established:

• Creatinase specifically degrades endogenous creatine (into sarcosine and urea) at the start.

• Sarcosine oxidase catalyzes sarcosine to generate H₂O₂.

• Catalase decomposes H₂O₂ into water and oxygen, preventing its involvement in subsequent Trinder reactions.

CAT’s interference-clearing effect is remarkable and has been widely applied in biochemical diagnostic reagents, as shown below:

3. Application Pain Points of Catalase

With its ability to efficiently decompose hydrogen peroxide, catalase is hailed as a “green multi-tasker” in food processing, textile bleaching, medical diagnostics, and environmental protection. However, in practice, this theoretically outstanding enzyme faces three major pain points: low activity, poor purity, and weak stability.

Pain Point 1: Low Activity — “Powerless” in Textile Bleaching

In the textile industry, catalase is used to remove residual hydrogen peroxide after bleaching to prevent uneven dyeing. One printing and dyeing factory purchased a batch of catalase with an enzymatic activity (U/mg) only 60% of the standard value. As a result, to treat the same amount of fabric, nearly double the enzyme was required and reaction time extended by 50%. This not only increased costs but also slowed production lines, causing delivery delays. Low activity directly dragged down efficiency, leaving the manufacturer frustrated: “Too costly to use, too risky to stop using.”

Pain Point 2: Poor Purity — “Safety Hazard” in Food Processing

The food industry (such as dairy sterilization and wine preservation) requires enzymes of very high purity, but commercial catalases often contain contaminant proteins or microbial residues. A yogurt factory once used a low-purity batch, and the impurities caused off-flavors in products. Insufficient purity not only reduced catalytic efficiency but also risked introducing allergens or toxins, posing both safety and reputational threats.

Pain Point 3: Poor Thermal Stability — The “Fragile Moment” in Diagnostics

In in vitro diagnostics, catalase is a critical reagent for glucose, uric acid, cholesterol, and other tests. However, catalase is highly temperature-sensitive. Studies show that catalase extracted from mussels lost about 30% of activity after 15 minutes at 45℃, and at 60℃ for 15 minutes, only 10.6% activity remained. Easy inactivation directly impacts storage, transportation, and shelf life of diagnostic kits.

Hzymes Catalase (HH2905)

Hzymes proudly presents the new generation of “Armored Catalase,” engineered to overcome the core pain points:

1. Purity Breakthrough
   SEC-HPLC purity ≥99% with excellent batch-to-batch consistency.

1. Enhanced Enzyme Activity
   Enzymatic activity is defined as the amount of enzyme that catalyzes the decomposition of 1 μmol H₂O₂ per minute at 37℃ and pH 7.0.

• Traditional bovine liver catalase: 2–5 KU/mg (up to 6 KU/mg after purification).
• Hzymes recombinant catalase (microbial expression, purification, lyophilization): ≥25 KU/mg for protein, ≥13 KU/mg for enzyme powder.

1. Superior Stability
   At 70℃, Hzymes CAT shows a half-life of 240 min (R²=0.987), compared with competitor A’s 14 min (R²=0.986).

1. Comprehensive Quality Control
   All batches undergo testing for impurities, microbial load, and side enzymes. Hzymes lyophilized catalase is rigorously evaluated for purity, moisture content, protein activity, enzyme powder activity, solubility, stability, microbial contamination, side enzyme presence, and diagnostic reagent validation.

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