CATALASE FROM PENICILLIUM NOTATUM

CAS: 977090-05-3 ANTIMICROBIAL AGENT, ENZYME, PROCESSING AID

Catalase from Penicillium notatum is a microbial enzyme preparation used as an antimicrobial agent and processing aid in food contexts, typically listed in the FDA Substances Added to Food inventory without specific numerical regulatory allowances.

What It Is

Catalase from Penicillium notatum refers to a preparation of the enzyme catalase derived from cultures of the filamentous fungus Penicillium notatum. Catalase itself is a protein enzyme whose primary biochemical function is the catalytic breakdown of hydrogen peroxide into water and oxygen, a reaction that is valuable for reducing residual oxidants during food processing and in other technological applications. The CAS Registry Number assigned to this enzyme preparation is 977090-05-3, which appears in inventory listings as a unique identifier associated with this substance in regulatory and technical databases. As an ingredient category, it falls under enzyme and antimicrobial agent classifications and is used as a processing aid in selected food applications under specific regulatory inventories. The organism source, fungal catalase, is nonpathogenic and used for its catalytic properties rather than direct nutritive value or flavor contribution. While catalase enzymes occur naturally in many living organisms, the industrial preparation from P. notatum is specifically adapted for technical uses that may include mitigating peroxide residues or supporting oxidative stability during food production.

How It Is Made

The manufacturing of catalase from Penicillium notatum generally involves fermentation of the Penicillium strain under controlled conditions optimized for enzyme secretion, followed by downstream processing to recover the catalase protein. In a typical process, the production organism is cultured in a nutrient medium to achieve high cell densities and enzyme expression, after which the fungal biomass and culture supernatant containing the enzyme are separated. Enzyme purification may include steps such as filtration, concentration, and drying to yield a stable powder form suitable for food industry use. Although specific production protocols may vary among manufacturers, good manufacturing practice principles are applied throughout to ensure product consistency and minimize contaminants. The resulting enzyme preparation is expected to meet established identity and purity criteria consistent with regulatory specifications for enzyme preparations used in food processing, although detailed modern monograph specifications for the P. notatum preparation itself are not readily public in commonly accessed regulatory compendia. Control of fermentation parameters and removal of unwanted microbial metabolites are typical components of quality assurance for enzyme production from microbial sources.

Why It Is Used In Food

Catalase from Penicillium notatum is used in food processing primarily for its ability to decompose hydrogen peroxide, which may be present as a residue from bleaching, sanitization, or other oxidative processing steps. By catalyzing the breakdown of hydrogen peroxide into benign end products, catalase aids in preventing oxidative damage to food components and can help preserve the quality and safety of products. This function is particularly useful in dairy and other sensitive food matrices where unwanted oxidants can affect sensory and nutritional qualities. The antimicrobial classification reflects the indirect effect of reducing oxidative stress that might otherwise allow spoilage organisms to proliferate under suboptimal conditions. As a processing aid, catalase facilitates technological objectives without imparting direct flavor, texture, or nutritional changes to the final product. Its enzymatic activity can complement other processing technologies by enhancing product stability and ensuring residual oxidants do not contribute to off-flavors or deteriorative reactions.

Adi Example Calculation

Illustrative calculation of Acceptable Daily Intake (ADI) is typically based on body weight and established numeric ADI values when available. Because no specific numeric ADI is published in major regulatory compendia for catalase from P. notatum, we cannot perform a numeric example calculation for this ingredient. In general terms, if an ADI of X mg per kg body weight were established, an individual weighing 70 kilograms would have a theoretical daily exposure threshold of 70 times X milligrams. However, in the absence of a confirmed numeric ADI, this remains an explanation of the concept rather than a calculable example specific to this enzyme preparation.

Safety And Health Research

Scientific research into catalase from microbial sources, including Penicillium notatum, has explored its use in different industrial applications, supporting its effectiveness in catalyzing hydrogen peroxide breakdown. The enzyme's safety profile as a processing aid is based on its biochemical nature as a protein and the history of enzyme use in food processing, with considerations focusing on potential allergenicity and microbial source safety. Regulatory assessments often examine the source organism to ensure that production strains are nonpathogenic and nontoxigenic, and that processes minimize residual contaminants in the final enzyme preparation. Scientific publications have also investigated dietary effects of exogenous catalase in animal models in agricultural research contexts, examining impacts on oxidative processes within biological tissues, though these studies are specific to research models rather than direct food additive evaluations. Safety evaluations for enzyme preparations typically include toxicology and exposure assessments, but specific health effect claims outside the intended processing functions are not established unless supported by regulatory findings.

Regulatory Status Worldwide

In the United States, catalase from Penicillium notatum is listed in the FDA's Substances Added to Food inventory (formerly known as EAFUS), which catalogues substances that have been reported for use in food, including those evaluated by external expert panels such as FEMA and JECFA. This listing indicates that the substance has been recognized for its technical function but does not by itself constitute a direct FDA regulatory approval with defined use conditions, and the FDA does not list specific use levels or limitations for this enzyme preparation in the Code of Federal Regulations. As an enzyme preparation, catalase is managed under general provisions that govern processing aids and indirect additives, with safety assessments informed by expert committees. Internationally, the Joint FAO/WHO Expert Committee on Food Additives (JECFA) provides specifications and reviews for many food additives, including enzymes, although specific evaluation details for catalase from P. notatum would need to be obtained from the searchable JECFA database. National regulations in various jurisdictions may treat enzyme preparations differently, but common principles require demonstration of safety and technical necessity before use in food processing contexts.

Taste And Functional Properties

Catalase itself does not contribute a distinct taste to food products because it is used in processing at levels where functional effects, rather than sensory attributes, are the primary concern. It acts catalytically, meaning that a relatively small amount of enzyme can have a substantial effect on hydrogen peroxide breakdown without remaining in the final product in functionally significant quantities. The enzyme typically exhibits activity across a range of temperatures and pH levels encountered in food processing, although catalytic efficiency can vary with changing conditions. Heat and extreme pH conditions can denature the enzyme, resulting in loss of activity, which is a functional consideration during processing design. Because catalase functions as a protein, its stability and solubility characteristics are similar to those of many other food enzymes: it is water-soluble and active in aqueous systems where substrate (hydrogen peroxide) is accessible. Enzyme preparations are typically formulated to retain activity under expected processing conditions, with manufacturers specifying recommended use conditions that align with intended technological purposes.

Acceptable Daily Intake Explained

Acceptable Daily Intake (ADI) is a risk assessment concept used by regulatory bodies to express the amount of a substance that can be consumed daily over a lifetime without appreciable health risk, based on toxicological data. For catalytic enzyme preparations like catalase, which are used at low levels and are proteins that are expected to be digested, specific ADIs are not always established in the same way as for conventional chemical additives. In instances where enzymes have been evaluated by expert committees, ADIs or other safety guidance may appear in regulatory monographs. However, for catalase from P. notatum, specific numeric ADI values are not readily available in authoritative additive specification databases, and therefore numerical guidance is generally not provided for consumers. The absence of a numeric ADI does not imply a safety concern, but rather reflects the nature of enzyme preparations and how they are assessed under prevailing regulatory frameworks.

Comparison With Similar Additives

Catalase from Penicillium notatum can be compared with other enzyme processing aids such as glucose oxidase and lipase, which also serve technical roles in food manufacturing. Glucose oxidase, for example, catalyzes the oxidation of glucose to hydrogen peroxide and can be used in baking to strengthen dough or in biosensor applications, illustrating how different enzymes provide targeted functions based on their substrate specificity. Lipases catalyze the hydrolysis of fats and are used in dairy modifications and flavor development. Compared to these, catalase primarily addresses oxidative residues rather than direct transformation of major food components. Each enzyme preparation has distinct catalytic properties, stability profiles, and application niches, all subject to regulatory evaluation as processing aids. While glucose oxidase from Penicillium species is widely characterized for its technological and regulatory status, catalase fits into the broader class of enzyme aids with specific technological roles and safety considerations.

Common Food Applications Narrative

Catalase from Penicillium notatum finds its primary applications in food processing contexts where hydrogen peroxide is used or formed during treatment steps that require sanitization or bleaching. In such contexts, catalase helps ensure that residual peroxide does not remain in the food matrix, thereby maintaining product quality and preventing oxidative damage to sensitive components. For example, in dairy processing, catalase can be applied following peroxide-based sanitation to decompose leftover oxidants before further heat treatment or packaging, contributing to smoother processing flows and consistent quality outcomes. In other enzyme-assisted processing steps, catalase may be included in formulations where a controlled reduction of oxidative compounds is necessary to protect color, texture, or nutrient profiles. The enzyme's action is often complementary to the broader suite of processing aids and stabilizing factors that food manufacturers use to achieve consistent, high-quality products. Although not all enzyme preparations are used in every segment of the food industry, catalase preparations such as those from P. notatum serve specific technical roles that fit into the broader ecosystem of food processing technologies.

Safety & Regulations

FDA

  • Notes: Listing in the Substances Added to Food inventory does not equate to specific FDA approval with defined use conditions.

EFSA

  • Notes: EFSA has published evaluations of food enzymes, but specific numeric ADI values for this preparation were not found in publicly accessible sources.

JECFA

  • Notes: Specific JECFA evaluation monograph or numeric ADI for this substance was not identified in the JECFA database.

Sources

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