CATALASE FROM ASPERGILLUS NIGER

CAS: 977031-84-7 ANTIMICROBIAL AGENT, ENZYME, PROCESSING AID

Catalase from Aspergillus niger is a food enzyme preparation produced by controlled fermentation that catalyzes the breakdown of hydrogen peroxide into water and oxygen and is used as an antimicrobial enzyme and processing aid.

What It Is

Catalase from Aspergillus niger is an enzyme preparation produced by fermentation of the fungus Aspergillus niger that facilitates the rapid decomposition of hydrogen peroxide into water and oxygen. As an enzyme, catalase falls into the class of oxidoreductases with the enzyme commission number EC 1.11.1.6, and because it facilitates this reaction without itself being consumed, it is widely used in food and industrial applications to remove residual hydrogen peroxide. In food processing contexts, this substance is used as an antimicrobial agent and processing aid to mitigate oxidative stress and reduce residual oxidants in food streams. This enzyme preparation is distinct from the catalase naturally present in living organisms, as it is manufactured and purified to meet food industry specifications. The enzyme’s activity is defined by its ability to catalyze the decomposition of hydrogen peroxide, and typical specifications for catalase preparations include defined activity units per milligram of protein. In regulatory inventories such as the U.S. Food and Drug Administration’s Substances Added to Food (formerly EAFUS), catalase from Aspergillus niger is listed with its CAS registry number 977031-84-7 and associated technical functions including antimicrobial agent, enzyme, and processing aid, indicating its recognized usage purposes in food formulations and processing contexts. This listing reflects its established technical roles rather than specific permitted use levels in every food category.

How It Is Made

Catalase from Aspergillus niger is manufactured using microbial fermentation, wherein a production strain of Aspergillus niger is cultured under controlled conditions to produce the catalase enzyme extracellularly. During this process, the fungus is grown in a nutrient medium where it secretes catalase into the broth; the resulting broth is then subjected to purification steps to isolate the enzyme preparation. Typical downstream processing can include filtration, concentration, and stabilization procedures to yield a catalase preparation that retains high enzymatic activity and is suitable for use in food manufacturing. The production of catalase involves controlling parameters such as pH, temperature, and aeration to optimize yield and enzyme quality, and ensuring the absence of viable production organism cells in the final enzyme preparation. Manufacturers adhere to good manufacturing practices and food safety quality systems to avoid contamination and ensure consistent product characteristics. Enzyme specifications for catalase typically define activity units per mass of protein, which provide a measure of catalytic potency, and the enzyme preparation is often characterized for its pH and temperature activity profiles to guide its use in food processes. Although the exact fermentation and purification protocols are proprietary to specific enzyme manufacturers, the overarching approach remains similar across the industry: use of safe microbial strains, optimization of production conditions, and rigorous purification and quality control to deliver a stable catalase enzyme suitable for industrial food applications. The resulting enzyme preparation is intended for use in line with good manufacturing practice and technical necessity.

Why It Is Used In Food

Catalase from Aspergillus niger is used in food manufacturing primarily because of its ability to rapidly break down hydrogen peroxide, which can be present in food process streams after bleaching or sterilization treatments. Hydrogen peroxide, while useful for microbial control in certain food ingredients, must be effectively removed before further processing or packaging to prevent residual oxidants that could affect food quality or safety. As an antimicrobial agent and processing aid, catalase serves to reduce residual oxidizing agents, thereby minimizing oxidative damage to food components, improving stability, and supporting product quality during subsequent processing stages. It is especially relevant in processes such as egg product processing, where hydrogen peroxide might be used for sanitization, or in cheese manufacture, where residual oxidants must be eliminated to support starter culture activity and product texture. Because catalase is an enzyme, its action is highly specific and efficient under appropriate conditions, enabling targeted decomposition of hydrogen peroxide at relatively low levels without introducing additional chemical residues. This makes it valuable in food production environments where chemical carryover must be minimized. Technical uses include neutralizing cleaning or sanitizing agents in food ingredients and supporting consistent product characteristics across batches. In many food manufacturing contexts, catalase preparations are used at levels necessary to achieve hydrogen peroxide breakdown in accordance with good manufacturing practice, emphasizing the enzyme’s functional role rather than its contribution of nutritional properties. Its use is driven by processing needs and quality objectives rather than direct sensory effects on the final food product.

Adi Example Calculation

Because catalase from Aspergillus niger does not have a codified Acceptable Daily Intake (ADI) assigned by major regulatory bodies, this section provides an illustrative, hypothetical calculation rather than a regulatory value. For example, in a safety assessment context, an expert panel might estimate dietary exposure in a population based on typical use levels of the enzyme preparation and food consumption data, expressing exposure in terms of total organic solids per body weight. If a hypothetical dietary exposure estimate were 1 milligram of total organic solids (TOS) per kilogram of body weight per day for an adult weighing 70 kilograms, the total daily exposure would be 70 milligrams of TOS. In toxicological studies in laboratory animals, safety endpoints such as a no observed adverse effect level (NOAEL) are identified and compared with exposure estimates to calculate a margin of exposure, which helps regulators understand the relationship between expected human exposures and levels that caused no adverse effects in test animals. Larger margins generally indicate broader safety buffers. This illustrative calculation does not prescribe a safe intake level for individuals and is not a regulatory ADI. It demonstrates how regulators use exposure estimates and toxicology data to contextualize potential risk, emphasizing that any specific intake advice must be grounded in formal regulatory evaluations rather than hypothetical examples.

Safety And Health Research

Safety assessments for catalase from Aspergillus niger have been conducted by scientific panels such as the European Food Safety Authority (EFSA), which evaluated toxicological data including genotoxicity tests and 90-day oral toxicity studies in laboratory animals to characterize risks associated with exposure to total organic solids of the enzyme preparation. These evaluations include analysis of potential for DNA damage and systemic toxicity over repeated exposure, and account for dietary exposure estimates based on intended uses in food production. In one EFSA opinion, findings showed no genotoxicity but identified a no observed adverse effect level in toxicology studies that, when compared with estimated exposure, led to discussion about margins of exposure and uncertainties in safety conclusions. Enzyme preparations like catalase are proteins that, when consumed, are typically digested in the gastrointestinal tract and broken down into amino acids, a property shared by many food enzymes used in processing. However, allergenicity potential is considered in safety evaluations because proteins from microbial sources can sometimes share sequence similarity with known allergens, and in some evaluations low likelihood but non-zero risk of allergic reaction by dietary exposure has been identified. Safety assessments also consider absence of viable production organisms in final preparations and the purity of the enzyme preparation to ensure contaminants are minimized. Overall, health research and regulatory reviews emphasize that safety evaluation of food enzymes encompasses multiple endpoints including genetic toxicity, systemic toxicity, and allergenic potential, with conclusions tailored to the specific enzyme preparation, production strain, and intended uses in food processes.

Regulatory Status Worldwide

In the United States, catalase from Aspergillus niger is listed in the FDA’s Substances Added to Food inventory (formerly EAFUS) with CAS number 977031-84-7 and recognized technical functions including antimicrobial agent, enzyme, and processing aid, and associated with specific food labeling and standards regulations in Title 21 of the Code of Federal Regulations concerning cheese and related products. Inclusion in the Substances Added to Food inventory indicates that the ingredient and its uses have been notified to FDA, although this listing does not by itself constitute an explicit FDA approval of specific use levels or industry-wide authorizations beyond good manufacturing practice context. The FDA has also acknowledged GRAS notices for enzyme preparations from Aspergillus niger that include catalase enzyme preparations based on common use in food and scientific procedures. However, catalase from Aspergillus niger is not separately codified with a distinct CFR section like some other enzyme preparations. In the European Union, food enzymes including catalase from Aspergillus niger must undergo a safety evaluation by the European Food Safety Authority (EFSA) and be included in an EU Community list for permitted food enzymes; EFSA published a scientific opinion on the safety evaluation of catalase produced by a non-genetically modified Aspergillus niger strain, indicating detailed assessment of toxicological and exposure data in relation to intended uses. Regulatory approval or inclusion in EU lists would be contingent on the outcome of such evaluations and appropriate authorization. For international oversight, bodies such as the Joint FAO/WHO Expert Committee on Food Additives (JECFA) have historically evaluated catalase from Aspergillus niger and reported that decisions on ADI were postponed in early evaluations, highlighting that expert committees may review enzyme preparations separately to determine specifications and safety considerations. Regulatory status worldwide varies by jurisdiction and typically reflects assessments of enzyme safety and technical necessity rather than broad numeric allowable intake figures.

Taste And Functional Properties

Catalase from Aspergillus niger itself does not contribute flavor, aroma, or visible sensory characteristics to food products; its primary functional property is enzymatic activity that catalyzes the decomposition of hydrogen peroxide into water and oxygen. Because the reaction products are neutral molecules already present in food and the enzyme acts on trace levels of residual oxidants, catalase is considered not to impart taste or odor impacts at normal use levels. Functionally, catalase exhibits optimal activity at near-neutral pH values and moderate temperatures compatible with many food processes. The enzyme’s catalytic efficiency allows for effective removal of hydrogen peroxide, which could otherwise contribute to oxidative degradation of sensitive food components or interfere with other biological processes such as fermentation. Catalase can operate within a range of conditions typical of food processing, making it a versatile processing aid where residual oxidants need to be addressed. Products containing catalase enzyme preparations should be formulated so that the enzyme is active under the relevant processing conditions and inactivated or removed before final product stabilization if necessary. While the enzyme itself is a protein and can be sensitive to heat and pH extremes, within the optimized conditions it facilitates its intended chemical transformation without modifying the sensory profile of the food. For consumers, the functional benefits of catalase manifest indirectly through improved product consistency rather than through direct sensory changes.

Acceptable Daily Intake Explained

An Acceptable Daily Intake (ADI) is a regulatory concept representing an estimate of the amount of a substance that can be ingested daily over a lifetime without appreciable health risk, derived from toxicological studies and incorporating safety factors. In the context of catalase from Aspergillus niger, specific numeric ADIs have not been established on a global regulatory basis because enzyme preparations are often evaluated on the basis of technical use levels and exposure estimates rather than being assigned formal ADI values like many low molecular weight additives. For enzyme preparations that have undergone formal evaluation by expert committees such as JECFA, early evaluations for catalase indicated that decisions on ADI were postponed, reflecting that sufficient data to set an ADI had not been concluded in those reviews. In regulatory assessments like those conducted by EFSA, safety margins are considered based on toxicological study endpoints relative to estimated human exposures, and regulators interpret these margins to assess whether typical use levels pose safety concerns under intended conditions of use without assigning a numerical ADI. In practical terms, this means that catalase enzyme preparations are managed through regulatory listings, expert safety evaluations, and good manufacturing practice rather than a specific numeric ADI, with oversight focusing on ensuring that enzyme use in food processing does not result in exposures that would raise safety issues for consumers.

Comparison With Similar Additives

Catalase from Aspergillus niger can be compared with other enzyme additives used in food processing such as glucose oxidase and lipase preparations. Like catalase, glucose oxidase is an oxidoreductase that modifies oxidants in food systems; glucose oxidase catalyzes the oxidation of glucose to hydrogen peroxide, and is used to improve dough properties in baking. Catalase and glucose oxidase are often considered complementary in systems where oxidative balance affects product quality. Lipase enzymes, by contrast, catalyze the hydrolysis of fats into free fatty acids and glycerol and are used in cheese flavor development and dairy processing. While lipases influence sensory properties through modification of lipid components, catalase serves a processing rather than flavor role, demonstrating how different enzyme classes can serve distinct technological functions in food. Another class of enzymes used in food applications includes amylases, which break down starches to sugars for texture and sweetness modulation in baked goods and other foods. Compared with catalase’s role in managing residual oxidants, amylases and lipases directly influence macronutrient transformations. These comparisons illustrate that enzyme additives vary widely in functional impact, with catalase’s primary role focused on oxidative management in food processing rather than direct macronutrient modification or flavor development.

Common Food Applications Narrative

Catalase from Aspergillus niger is used across a variety of food manufacturing contexts where residual hydrogen peroxide must be broken down to ensure product quality and process safety. In egg processing, for example, hydrogen peroxide may be used in sanitization steps, and catalase assists in removing remaining oxidants before further handling to protect functional properties of egg proteins. In cheese production and other dairy applications, catalase helps mitigate oxidants that could affect starter culture performance and product texture. In cereal-based processing and baked goods, catalase can play a role where bleaching agents or oxidants are used upstream, supporting consistent dough behavior and final product attributes by removing residual chemical oxidants. Vegetable and fruit juice manufacturing also uses catalase to eliminate trace hydrogen peroxide from sanitizing treatments, helping maintain fresh taste and color. Catalase can also be part of enzyme blends used in processing streams where multiple transformations are required, and as such it contributes to overall process efficiency and product quality rather than to direct sensory attributes. Its use is guided by the technical necessity to manage oxidative agents in food systems and is integrated into processing sequences in line with good manufacturing practice, supporting reliable outcomes in a range of food categories.

Safety & Regulations

FDA

  • Notes: Included in FDA Substances Added to Food inventory; specific regulatory approval text not codified in CFR for catalase fraction. FDA has recognized GRAS notices for related enzyme preparations but direct CFR permission sections for catalase as an enzyme preparation are not explicitly verifiable.

EFSA

  • Notes: EFSA has evaluated catalase enzyme safety in scientific opinions, but specific e number or numeric ADI was not assigned in the d opinion.

JECFA

  • Notes: JECFA evaluated catalase from Aspergillus niger and reported decision on ADI postponed; no numeric ADI was established in the d evaluation.

Sources

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