Team Chemistry -
Created by: Team Chemistry -, Last Updated: April 25, 2024


Catalase is a fascinating enzyme found in nearly all living organisms that are exposed to oxygen. This complex compound plays a critical role in protecting cells by breaking down hydrogen peroxide, a potentially harmful byproduct of cellular processes, into water and oxygen. By doing so, catalase helps maintain cellular health and prevents damage to tissues. This enzyme is essential in the study of chemistry, as it showcases how specific proteins work within living systems to manage chemical reactions. Its ability to rapidly convert harmful substances into harmless ones highlights the importance of biochemical processes in our daily lives.

What is Catalase?

Catalase is an enzyme found in nearly all living organisms that are exposed to oxygen. Its primary function is to break down hydrogen peroxide, a harmful byproduct of metabolic processes, into water and oxygen. This reaction is crucial because it helps protect cells from oxidative damage. The chemical formula for catalase is 𝐹𝑒(𝐸)(𝑂𝐻)(𝑂2)

Types of Catalase

Catalase enzymes vary slightly depending on the organism they are found in, but primarily, they can be classified into three main types: typical catalases, catalase-peroxidases, and manganese catalases. Each type serves the fundamental role of breaking down hydrogen peroxide into water and oxygen but differs slightly in their structure and the additional functions they perform.

Typical Catalases

Typical catalases are the most common form found in animals, plants, and fungi. They are highly efficient and focus solely on converting hydrogen peroxide into less harmful substances to prevent cell damage.


Catalase-peroxidases are more versatile and found mainly in bacteria and archaea. In addition to breaking down hydrogen peroxide, they can also act on other peroxides, serving a dual function which makes them crucial for the survival of these organisms in harsh environments.

Manganese Catalases

Manganese catalases, instead of containing iron in their active sites like the other types, contain manganese. This type is less common and is typically found in bacteria that need to adapt to very high levels of hydrogen peroxide. Manganese catalases help these bacteria manage oxidative stress differently from organisms that contain the more typical iron-based catalases.

Structure of Catalase


Catalase is a large, complex enzyme made up of four identical subunits, each containing an iron-containing heme group. This heme group is crucial for the enzyme’s ability to process hydrogen peroxide into water and oxygen. Each subunit is not just a simple chain but folds into a unique shape that allows the enzyme to function effectively. The structure of catalase is designed to maximize its efficiency, allowing it to react with millions of hydrogen peroxide molecules every second. This makes catalase extremely effective at protecting cells from oxidative damage.

Physical Properties of Catalase

Molecular WeightApproximately 250,000 grams per mole; varies slightly depending on the source organism.
Optimal pHRanges from 7.0 to 11.0, optimal around pH 7.0 for most catalases.
Optimal TemperatureGenerally 37°C (98.6°F), though stability can range from 30°C to 60°C (86°F to 140°F).
SolubilitySoluble in water, facilitating its function in the cellular environment.
StabilityStable under normal physiological conditions; loses activity when exposed to high concentrations of hydrogen peroxide.
AppearanceColorless to slightly brown, crystalline solid when purified.

Chemical Properties of Catalase

Catalytic Activity

Catalase significantly accelerates the decomposition of hydrogen peroxide into water and oxygen, a crucial reaction for shielding cellular components from oxidative harm. The reaction can be summarized by the chemical equation:

2H₂O₂ → 2H₂O + O₂

This illustrates how catalase converts two molecules of hydrogen peroxide into two molecules of water and one molecule of oxygen.

Substrate Specificity

Although primarily known for its action on hydrogen peroxide, catalase can occasionally catalyze the oxidation of other small molecules in the presence of hydrogen peroxide, thereby acting as a peroxidase.

Iron Coordination

The active site in catalase contains a heme group, central to which is an iron ion. This iron is essential for the enzyme’s interaction with hydrogen peroxide and alternates between the Fe(III) and Fe(IV) oxidation states during the reaction process.

pH Sensitivity

Catalase operates best within a specific pH range, generally around pH 7.0, showing optimal activity. Its effectiveness decreases when the pH deviates from this range, highlighting its sensitivity to environmental changes.

Thermal Stability

Catalase maintains stability and remains active within certain temperature limits, usually around 37°C (98.6°F), which aligns with the body temperature of many living organisms, including humans.

Functions of Catalase


Decomposition of Hydrogen Peroxide

The primary function of catalase is to catalyze the rapid decomposition of hydrogen peroxide into water and oxygen. This is vital because hydrogen peroxide is a toxic byproduct of many metabolic reactions and can cause cellular damage if not removed.

Protection from Oxidative Stress

By breaking down hydrogen peroxide, catalase helps protect cells from oxidative stress. This stress can lead to cell death and has been linked to various diseases, including cancer and neurodegenerative disorders. Catalase mitigates these risks by ensuring that hydrogen peroxide levels remain low.

Signal Regulation

Recent studies suggest that catalase can also play a role in cellular signaling by modulating the levels of hydrogen peroxide. Hydrogen peroxide acts as a signaling molecule in various biological processes, and by controlling its concentration, catalase influences processes like cell growth, cell death, and response to stress.

Antioxidant Defense

Catalase acts as an antioxidant by removing hydrogen peroxide, thus preventing it from being converted into more reactive oxygen species (ROS) by other enzymes like myeloperoxidase. This activity contributes to the overall antioxidant defense system of the body, which protects against a range of oxidative damages.

Examples of Catalase


Human Liver

The liver has lots of catalase. This enzyme breaks down hydrogen peroxide that forms when harmful substances are detoxified, helping to protect liver cells.

Blood Cells

Red blood cells contain catalase. It protects these cells and the circulatory system from the hydrogen peroxide generated in metabolism.


Bacteria such as Escherichia coli, have catalase. It defends them from oxidative stress and attacks by the host’s immune system.

Plant Cells

Catalase is in the peroxisomes of plant cells. It handles hydrogen peroxide from photorespiration, a process that involves taking in oxygen and releasing carbon dioxide in light.


Fungi like yeasts use catalase to manage oxidative stress during their metabolism, especially when they break down sugars without oxygen.

Catalase: Effects on Human Body

  • Reduces Oxidative Stress: Catalase breaks down Hydrogen Peroxide into water and oxygen, significantly reducing oxidative stress in cells. This process prevents cellular damage and promotes longevity.
  • Protects Cells: By transforming harmful hydrogen peroxide into harmless substances, catalase helps protect cells throughout the body. This is crucial for cell health and function.
  • Supports Liver Function: The liver, which detoxifies chemicals and metabolizes drugs, produces Hydrogen Peroxide. Catalase in the liver helps break down this compound, aiding in liver health and function.
  • Enhances Healing: Catalase contributes to the body’s healing processes. By controlling hydrogen peroxide levels, it helps manage inflammation and repair tissue damage.
  • Prevents Disease Development: Lower levels of oxidative stress and reduced cellular damage contribute to a decreased risk of diseases, including cancers and neurodegenerative disorders.


How Does Catalase Increase the Rate of Reaction?

Catalase increases reaction rates by breaking down hydrogen peroxide into water and oxygen rapidly, enhancing metabolic efficiency.

What is the optimal Temperature for Catalase?

The optimal temperature for catalase activity is around 37°C (98.6°F), typical for human body temperature.

At What pH Level Does Catalase Work?

Catalase functions best at a pH around 7.0, typical for most intracellular environments.

What Does Catalase Do in Food?

In food, catalase helps prevent oxidation, extending shelf life and preserving color and flavor.

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