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What Foods Contain Asparaginase? The Surprising Truth About This Enzyme

4 min read

Asparaginase is most commonly known as a food additive, with studies showing it can reduce acrylamide formation by over 80% in some processed foods. However, few foods naturally contain asparaginase, with the enzyme primarily found in certain plants and microorganisms.

Quick Summary

The enzyme asparaginase is rarely found naturally in common foods, though certain plants and microorganisms contain it. Commercially, it is intentionally added to processed foods to reduce the formation of acrylamide.

Key Points

  • Not found in most common foods: Asparaginase is an enzyme that is not widely present in the foods we typically eat, unlike the amino acid asparagine.

  • Natural sources exist: Specific plants, such as asparagus, tamarind, and green chillies, naturally contain asparaginase.

  • Microbial production is standard: The asparaginase used commercially is produced from microorganisms, primarily bacteria like Bacillus subtilis and fungi like Aspergillus oryzae.

  • Used as a processing aid: In the food industry, asparaginase is added to raw ingredients to break down asparagine and prevent the formation of acrylamide during cooking.

  • Reduces acrylamide in processed foods: Treating foods like potatoes, baked goods, and coffee with asparaginase significantly lowers the level of acrylamide, a potential carcinogen.

  • Distinguish from asparagine: Don't confuse foods that are high in the amino acid asparagine (like meat, dairy, potatoes) with those containing the enzyme asparaginase.

  • A food safety tool: The use of asparaginase is a modern food safety application designed to minimize the health risks associated with high-temperature food processing.

In This Article

Asparaginase vs. Asparagine: Clarifying the Crucial Difference

Before delving into specific food sources, it is vital to distinguish between asparaginase, an enzyme, and asparagine, an amino acid. Asparagine is a naturally occurring amino acid found widely in many plant and animal proteins, such as poultry, beef, dairy, and whole grains. Asparaginase is the enzyme that breaks down asparagine. This enzyme has gained attention primarily for its industrial application: when added to foods during processing, it hydrolyzes asparagine, thus preventing the formation of acrylamide during high-temperature cooking like frying and baking.

Therefore, most foods do not contain active asparaginase. The asparaginase activity found in food is almost exclusively due to the intentional addition of commercially produced, microbial-sourced enzymes. This is a critical distinction, as some people may confuse foods that are high in the precursor amino acid (asparagine) with foods containing the enzyme itself.

Natural Sources of Asparaginase: Plant and Microbial Origins

While industrial applications rely on microbial sources, some organisms naturally produce asparaginase.

Asparagus

The most direct and commonly cited food example is asparagus. The name asparaginase is even derived from the plant's genus, Asparagus. One study noted that asparaginase activity is significantly higher in the roots of Asparagus officinalis L. than in the spears and leaves, though it is present in all parts. While cooking would likely inactivate much of this heat-sensitive enzyme, its natural presence is a key part of the plant's metabolism.

Other Plant Sources

Plant-based asparaginase has been explored for its potential therapeutic benefits and for producing alternative enzymes with fewer side effects than microbial versions. Examples include:

  • Tamarind and Green Chillies: These contain high amounts of L-asparaginase.
  • Yellow Lupine (Lupinus luteus): A detailed study of this legume identified a specific type of asparaginase, though its primary function in the plant might be different than previously thought.
  • Tomato (Solanum lycopersicum): Researchers have found L-asparaginase activity in the fruit pulp of tomatoes, suggesting its potential use as a nutraceutical.
  • Soybean debris: Some studies indicate that asparaginase derived from soybean debris can be more efficient and stable than microbial versions for certain applications.

Microbial Sources

For most commercial and medical applications, asparaginase is produced by microorganisms in a controlled setting. These are not inherent food components but are produced and added during food processing. Key examples include:

  • Escherichia coli and Erwinia sp.: These bacteria are the primary sources for medical-grade L-asparaginase used in cancer treatments.
  • Aspergillus niger and Aspergillus oryzae: These fungi are widely used in the food industry to produce commercial asparaginase, such as the products PreventASe® and Acrylaway®.
  • Bacillus subtilis: This bacterium is a source for asparaginase used in food processing to mitigate acrylamide formation.

Commercial Application of Asparaginase in Processed Foods

The primary reason consumers encounter asparaginase in food is its role as a processing aid. The enzyme is added to raw materials, particularly starchy foods, to reduce the formation of the potentially carcinogenic compound acrylamide, which forms during high-temperature cooking via the Maillard reaction. The enzyme breaks down the amino acid asparagine, a key precursor to acrylamide, before it can react with reducing sugars.

Some common products treated with asparaginase include:

  • Baked goods: Bread, biscuits, and crackers.
  • Fried potato products: French fries and potato chips.
  • Snack foods: Extruded snacks and coffee.

What foods contain asparagine vs. asparaginase?

It is important to remember that most common foods contain asparagine, the amino acid, rather than the asparaginase enzyme. The list below highlights this critical distinction.

  • Foods High in Asparagine (No Asparaginase):

    • Poultry, beef, eggs, and dairy products.
    • Asparagus (contains some enzyme, but mostly the amino acid).
    • Potatoes, cereals, and baked goods (often have added enzyme, but naturally contain the amino acid).
    • Legumes, nuts, and seeds.
  • Foods with Added Asparaginase (Typically Microbial-Sourced):

    • Some commercially processed French fries and potato chips.
    • Certain industrial baked goods, including crackers and breads.
    • Some roasted coffee products.
    • Various other starchy, high-heat processed snacks.

Comparison of Natural vs. Commercial Asparaginase

Feature Natural Asparaginase (e.g., from Asparagus) Commercial Asparaginase (e.g., from Aspergillus)
Source Plants, microorganisms, animals Microorganisms (bacteria, fungi, yeast), grown in industrial fermentation tanks
Presence in Food Trace amounts, part of the organism's biology Added deliberately as a processing aid to reduce acrylamide
Active Form in Food Likely denatured and inactivated during cooking Active during food processing, then mostly inactivated by subsequent heat treatments
Purpose Naturally occurring metabolic function Food safety measure to reduce potential carcinogen formation
Specificity Can have varying specificity and activity levels depending on the source species Often engineered for high specificity and efficacy in food processing environments

The Role of Asparaginase in Food Safety

The intentional use of asparaginase in food processing is a significant step in food safety. Acrylamide, classified as a probable human carcinogen, is a major concern in high-temperature processed foods. By treating ingredients like potatoes and flour with asparaginase before cooking, the food industry can drastically lower acrylamide levels without altering the product's taste or texture. This proactive enzymatic approach offers a reliable method for mitigating potential health risks associated with certain everyday foods. The ability to use this enzyme to modify food composition safely highlights a fascinating area of food science and biotechnology.

Conclusion

While the search for foods that naturally contain asparaginase points to specific plant sources like asparagus, tamarind, and green chillies, the more common interaction with this enzyme occurs through commercial food processing. The primary purpose of adding microbially-sourced asparaginase to processed foods is not to increase its nutritional content but to serve as a critical food safety measure, reducing the formation of acrylamide during high-temperature cooking. As consumers, understanding this distinction helps demystify food labels and modern food production techniques. The use of enzymes like asparaginase showcases how science is continually applied to make our food supply safer and healthier.

For a deeper dive into the science of asparaginase, its production, and application, consult research from reputable sources like the National Institutes of Health.

Frequently Asked Questions

Asparaginase is added to foods like bread, fries, and chips to reduce the formation of acrylamide. During high-temperature cooking, the enzyme breaks down the amino acid asparagine, which would otherwise react with sugars to form acrylamide.

Yes, commercial asparaginase used in food is considered safe by regulatory bodies like the FDA, which has labeled it as 'Generally Recognized As Safe' (GRAS). It is a processing aid and does not negatively impact the food's taste or texture.

Asparagine is an amino acid that occurs naturally in many plant and animal foods. Asparaginase is an enzyme that catalyzes the breakdown of asparagine into aspartic acid and ammonia.

No, potatoes do not naturally contain significant amounts of asparaginase. However, they are high in asparagine and sugars, which is why commercial asparaginase is often added during the processing of products like potato chips and French fries to reduce acrylamide.

While trace amounts of asparaginase are found in specific plants like asparagus, tamarind, and green chillies, these are not reliable or potent dietary sources. The active enzyme used for food safety and medical applications comes from microbial production.

Yes, a different form of asparaginase (often from bacterial sources like E. coli) is used as a chemotherapeutic agent to treat certain cancers, particularly acute lymphoblastic leukemia.

Yes, asparaginase, like most enzymes, is sensitive to heat. The high temperatures used in cooking and baking would inactivate any naturally occurring or added enzyme, preventing it from having a prolonged effect.

References

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Medical Disclaimer

This content is for informational purposes only and should not replace professional medical advice.