AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS

CAS: 977172-57-8 ENZYME

AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS is an enzyme preparation derived from the bacterium Lactococcus lactis used in food processing to hydrolyze proteins under current good manufacturing practice conditions.

What It Is

AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS is a protein-hydrolyzing enzyme derived from the bacterium Lactococcus lactis. It belongs to a class of enzymes called aminopeptidases, which cleave amino acids from the N-terminal ends of peptide chains. These enzymes are often used in food processing to modify proteins. The CAS Registry Number associated with this ingredient is 977172-57-8, and other names include AMINOPEPTIDASE and LACTOCOCCUS LACTIS to reflect its enzymatic origin. In regulatory contexts, similar enzyme preparations derived from this organism are listed as affirmed GRAS ingredients under 21 CFR 184.1985 when used according to good manufacturing practice for protein hydrolysis and flavor development. The technical function of this ingredient is categorized as an enzyme that can catalyze peptide bond hydrolysis, potentially changing the functional properties of food proteins. Its classification as an enzyme preparation reflects its role as a processing aid rather than a nutritive component.

How It Is Made

The production of AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS begins with cultivation of the microorganism Lactococcus lactis under controlled fermentation conditions. Lactococcus lactis is a nonpathogenic lactic acid bacterium widely used in dairy fermentations. During fermentation, the bacteria express proteolytic systems that include aminopeptidases capable of hydrolyzing peptide bonds at the amino terminus of proteins. After fermentation, the enzyme preparation is separated from the biomass and other cellular components using standard downstream processing steps, which may include filtration, concentration, and purification. In some industrial processes, the enzyme may be further formulated or stabilized for consistent activity. Specifications for enzyme preparations often reference established compendia such as the Food Chemicals Codex, which provide criteria for purity, activity, and microbial limits. Enzyme preparations are typically produced to achieve consistent catalytic activity and meet food-grade quality standards. The final preparation is intended to contain the active aminopeptidase enzyme along with other peptidases that contribute to protein hydrolysis, and it is used under conditions of good manufacturing practice for its intended technological effects.

Why It Is Used In Food

AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS is used in food production primarily for its ability to hydrolyze proteins into smaller peptides and amino acids. This enzymatic hydrolysis can contribute to flavor development, improved solubility of proteins, and alteration of texture in processed foods. Because proteins can impart bitterness or limited solubility when intact, controlled enzymatic hydrolysis may enhance desirable sensory characteristics or facilitate the creation of specific protein hydrolysates with tailored properties. Within cheese manufacturing and other dairy fermentations, the proteolytic system of Lactococcus lactis naturally contributes to the breakdown of milk proteins, which is important for flavor and texture development during ripening. The addition of isolated enzyme preparations derived from this organism can accelerate or modify these processes. In broader food applications, aminopeptidase activity may be applied in the preparation of protein hydrolysates used in formulated foods where improved digestibility, reduced allergenicity, or specialized functional properties are desired. Its use is guided by current good manufacturing practice to achieve the intended technological effect without compromising food safety.

Adi Example Calculation

Because a numeric ADI value for AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS was not identified in authoritative regulatory evaluations consulted for this summary, an ADI-based calculation example cannot be provided. Instead, regulatory recognition under conditions of current good manufacturing practice serves as the basis for safe use, and exposure estimates consider the nature of processing aids, which are typically not present at significant levels in the finished food product after processing steps that inactivate enzyme proteins.

Safety And Health Research

Safety evaluations for enzyme preparations such as AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS typically consider the nonpathogenic nature of the source organism, the manufacturing process, and any potential residual activity in the finished food. Lactococcus lactis is widely used in dairy fermentations and is generally recognized as safe in the context of food production. Regulatory listings like 21 CFR 184.1985 reflect expert assessments that enzyme preparations derived from this organism do not present toxicological concerns when used under conditions of current good manufacturing practice. Toxicological studies for enzyme preparations often include assessments of microbial safety, potential allergenicity of the enzyme protein itself, and absence of contaminants. Because enzyme proteins are typically denatured during food processing, residual enzymatic activity in the final food is minimal. Research on aminopeptidases in general explores their catalytic properties and roles in protein modification rather than direct physiological effects upon consumption, as these enzymes act on food proteins during processing rather than in the gastrointestinal tract. Overall, the safety profile of enzyme preparations from Lactococcus lactis is supported by their long history of safe use in food fermentations and regulatory recognition in specific jurisdictions.

Regulatory Status Worldwide

In the United States, enzyme preparations derived from Lactococcus lactis that contain aminopeptidase are listed in the Code of Federal Regulations as substances affirmed as generally recognized as safe (GRAS) under 21 CFR 184.1985 when used as enzyme preparations according to current good manufacturing practice. This regulation describes the ingredient derived from the nonpathogenic, nontoxicogenic organism Lactococcus lactis and notes its use for flavor development in cheese manufacture and preparation of protein hydrolysates under good manufacturing practice conditions. The specific CFR citation reflects its regulatory recognition without numerical use limitations when applied appropriately. Outside the United States, regulatory assessments for enzyme preparations vary by jurisdiction, with many regulatory authorities evaluating enzyme preparations on the basis of source organism safety, production methods, and intended use. The Joint FAO/WHO Expert Committee on Food Additives (JECFA) provides a database of food additive specifications, though a specific numeric evaluation entry for this ingredient was not identified in the authoritative databases searched at the time of this summary. National regulatory frameworks in other regions may reference similar considerations for enzyme preparations used in food processing, focusing on organism safety and enzyme function.

Taste And Functional Properties

AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS itself does not impart a specific taste profile, but the products of its enzymatic activity—peptides and free amino acids—can influence flavor. The hydrolysis of proteins by aminopeptidases releases amino acids such as glutamate and aspartate, which can contribute to savory and umami taste notes in foods. Functional properties of the enzyme preparation include stability under processing conditions that are compatible with food manufacturing, such as specific ranges of temperature and pH where catalytic activity is maintained. Enzyme stability and activity can vary depending on formulation and processing parameters, and manufacturers typically characterize the enzyme preparation to ensure consistent performance in the intended application. The enzyme’s solubility and catalytic efficiency contribute to its function as a processing aid. Because it targets peptide bonds at the amino terminus, it acts synergistically with other proteases that may cleave internal peptide bonds, facilitating comprehensive protein modification where desired. The enzyme does not itself remain active in the finished food product if conditions such as heat treatment denature it during processing.

Acceptable Daily Intake Explained

Acceptable daily intake (ADI) values are established by regulatory bodies like JECFA when there is a need to quantify exposure for food additives with toxicological endpoints. For enzyme preparations such as AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS, no specific numeric ADI has been established in the authoritative sources consulted for this summary. In cases where regulators do not assign a numeric ADI, safe use is often based on the intrinsic safety of the source organism and the enzyme’s function, combined with the fact that the enzyme is used under current good manufacturing practice and is largely inactivated during processing. The concept of ADI provides a conservative estimate of the amount of a substance that can be consumed daily over a lifetime without appreciable risk, but such values are not always needed for ingredients with established safety through long-standing use and regulatory affirmation. In the absence of a numeric ADI, regulatory frameworks rely on conditions of use and manufacturing controls to ensure safety.

Comparison With Similar Additives

AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS shares functional characteristics with other proteolytic enzyme preparations used in food processing, such as proteases derived from microbial sources like Aspergillus oryzae and Bacillus subtilis. These enzyme preparations are all used to modify protein structures, enhance flavor development, or improve functional properties of food proteins. Compared with broad-spectrum proteases, aminopeptidases focus on cleaving amino acids from the N-terminal end of peptide chains, which can complement endopeptidases that cut internal peptide bonds. Another similar additive category includes microbial lipases used to alter fat components in cheese ripening, which, like proteolytic enzyme preparations, act as processing aids with specific catalytic roles. The choice among these enzyme preparations depends on the desired technological effect, such as flavor enhancement or texture modification, and regulatory status under local food additive regulations.

Common Food Applications Narrative

AMINOPEPTIDASE FROM LACTOCOCCUS LACTIS is used in various food manufacturing settings where controlled protein hydrolysis can contribute to desirable sensory or functional outcomes. In dairy fermentations, the proteolytic system naturally present in starter cultures, including aminopeptidase activity, plays an important role in flavor and texture development as cheese ages. Adding purified enzyme preparations derived from Lactococcus lactis offers manufacturers an option to influence these processes more directly. Outside dairy products, aminopeptidase preparations may be used in the production of protein hydrolysates employed as ingredients in formulated foods where enhanced protein solubility or tailored amino acid profiles are advantageous. The enzymatic action can help reduce bitterness associated with intact proteins and generate peptides that contribute to umami or savory flavor profiles. Because these enzyme preparations are used under conditions of good manufacturing practice, their inclusion in food processing is designed to achieve specific technological effects without remaining active in the finished product after any heat treatments. The narrative for consumers and food professionals highlights the ingredient’s role as a processing aid that supports protein modification and flavor development in a range of applications, consistent with its regulatory status in the United States.

Safety & Regulations

FDA

  • Approved: True
  • Regulation: 21 CFR 184.1985

EFSA

  • Notes: No specific EFSA numeric evaluation identified

JECFA

  • Notes: No specific JECFA evaluation entry found

Sources

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