Aminopeptidase
Enzyme Preparations
Flavoring Agents
9031-94-1
$14.69 ~ $22.04
Food
Free sample from 100g(NF)
One unit of:25kg/barrel
One unit of:25kg/barrel
25kg/barrel
Product Info
What is Aminopeptidase?
Aminopeptidase is an enzyme that cleaves single amino acids from the $ ext{N}$-terminus of proteins and peptides, primarily used in the food industry to modify protein flavor and texture through hydrolysis.
How is Aminopeptidase made?
| Step No. | Production Stage | Key Action | Control Point & Note |
|---|---|---|---|
| 1 | Inoculum Preparation | Select a high-yield microbial strain (e.g., Aspergillus oryzae) and cultivate it in a sterile seed medium to generate a healthy starter culture. | Control Point: Strain purity and culture viability. The inoculum must be free from contaminants and in the active growth phase to ensure a robust start to the main fermentation. |
| 2 | Large-Scale Fermentation | Transfer the seed culture into a large, sterilized bioreactor containing a production medium rich in nutrients. | Control Point: Strict control of pH, temperature, dissolved oxygen, and agitation. These parameters are continuously monitored to maximize the expression of Aminopeptidase enzyme by the microorganism. |
| 3 | Harvest & Cell Separation | Stop the fermentation process at the point of peak enzyme production. Separate the cells from the fermentation broth using centrifugation or microfiltration. | Control Point: Timing of the harvest is critical and determined by regular activity assays. The process is conducted at low temperatures to prevent enzyme degradation. |
| 4 | Extraction & Clarification | If the enzyme is intracellular, lyse the cells to release it. Clarify the crude enzyme solution (broth or lysate) by removing cell debris and other solids. | Control Point: Efficiency of cell lysis (if applicable) and removal of solids. Use high-speed centrifugation or depth filtration. The clarity of the solution impacts the efficiency of downstream purification. |
| 5 | Concentration & Diafiltration | Concentrate the clarified enzyme solution and remove small molecule impurities using Ultrafiltration (UF) membranes. | Control Point: Monitor membrane flux and transmembrane pressure to avoid fouling. This step significantly reduces volume and prepares the enzyme for chromatography by placing it in the correct buffer. |
| 6 | Chromatographic Purification | Pass the concentrated solution through one or more chromatography columns (e.g., ion-exchange, hydrophobic interaction) to separate the Aminopeptidase from other proteins. | Control Point: Monitor the protein elution profile (A280nm) and collect fractions. Assay fractions for specific activity to pool the purest, most active enzyme. This is the key step for achieving high product purity. |
| 7 | Formulation & Standardization | Add stabilizing agents (e.g., glycerol, salts) to the purified enzyme pool and dilute with a formulation buffer to a precise target activity level. | Control Point: Final enzyme activity assay must be performed accurately to ensure the product meets specifications. Stabilizers are crucial for the product's shelf-life and performance. |
| 8 | Sterile Filtration & Packaging | Pass the final formulated product through a 0.22 µm filter for sterilization and aseptically fill it into pre-sterilized containers in a cleanroom environment. | Control Point: Integrity of the sterile filter and the aseptic filling process. Final QC checks for microbial contamination, activity, and purity are performed on the packaged product before release. |
Technical Specifications
| CAS Number | 9031-94-1 |
| Solubility | Soluble in water; insoluble in organic solvents |
| Storage Conditions | Store sealed, cool, dry, away from light |
| Shelf Life | 12 Months |
Applications & Usage
Common Applications:
Debittering protein hydrolysate
thorough protein hydrolysis
bioactive peptide preparation
brewing clarity
feed digestibility
Mechanism of action:
| Parameter | Aminopeptidase |
|---|---|
| Functional Category | Enzymatic Processing Aid; Flavor Development Agent; Protein Hydrolysis Agent |
| Key Ingredients | Enzyme: Aminopeptidase (an exopeptidase typically derived from microbial sources such as *Aspergillus oryzae* or bacterial strains) |
| Mechanism of Action | Catalyzes the sequential hydrolysis of peptide bonds, cleaving single amino acids from the N-terminus of proteins and peptides. This action releases free amino acids (FAAs), which act as flavor precursors for umami and Maillard reactions, and effectively reduces bitterness by breaking down bitter-tasting short-chain hydrophobic peptides. |
| Application Effect in Product | Accelerated flavor development and maturation in aged cheese and fermented products (e.g., soy sauce, miso). Enhanced savory/umami taste in protein-rich foods, sauces, and soups. Reduction of bitterness in protein hydrolysates (whey, soy, casein) and yeast extracts. Increased degree of hydrolysis for specific protein modifications. |
Comparison:
| Product Name | Category/Type | Key Features | Strengths (vs peers) | Weaknesses (vs peers) | Best Use Cases | Why Choose |
|---|---|---|---|---|---|---|
| Aminopeptidase | Exopeptidase (N-terminal) | Sequentially cleaves single amino acids from the N-terminus of a peptide. | Allows for controlled, stepwise degradation from one specific end; useful for N-terminal sequencing. | Ineffective on proteins with a blocked N-terminus; slow for complete protein digestion. | Protein sequencing, removal of N-terminal tags (e.g., methionine), debittering of protein hydrolysates. | For specific analysis or modification of the N-terminus without disrupting the internal peptide sequence. |
| Carboxypeptidase | Exopeptidase (C-terminal) | Sequentially cleaves single amino acids from the C-terminus of a peptide. | The direct counterpart to aminopeptidase for C-terminal analysis; confirms full-length protein synthesis. | Ineffective on proteins with a modified C-terminus; slow for bulk digestion. | C-terminal protein sequencing, confirming protein sequence and integrity. | For specific analysis or modification of the C-terminus. |
| Trypsin | Endopeptidase (Serine protease) | Cleaves peptide chains internally after Lysine (K) or Arginine (R) residues. | Highly specific, efficient, and robust; generates predictable peptide fragments ideal for mass spectrometry. | Does not provide information about termini; produces a complex mixture of peptides rather than sequential data. | Proteomics (protein identification), large-scale protein digestion, detaching adherent cells in culture. | When you need to rapidly and reliably digest a protein into smaller, predictable fragments for analysis. |
| Chymotrypsin | Endopeptidase (Serine protease) | Cleaves peptide chains internally after large hydrophobic amino acids (F, W, Y). | Complements Trypsin's specificity, allowing for greater sequence coverage when used together. | Cleavage can be less specific than Trypsin; useless for direct terminal analysis. | Proteomics, generating different peptide maps from a protein, structural analysis. | To obtain different peptide fragments than Trypsin or to cleave proteins lacking Lys/Arg residues. |
| Pepsin | Endopeptidase (Aspartic protease) | Cleaves non-specifically after hydrophobic/aromatic residues at very low pH (1.5-2.5). | Uniquely active in highly acidic conditions where other proteases are denatured. | Low specificity results in a large number of small, unpredictable fragments; inactive at neutral pH. | Simulating gastric digestion, creating F(ab')2 antibody fragments, sample prep for certain analyses. | When digestion must occur in a highly acidic environment. |
Technical Documents
Available Documentation
Spec Sheet, Activity report, MSDS available
Safety Data Sheet (SDS)
MSDS available
Certificate of Analysis (COA)
Quality assurance documentation
Technical Data Sheet
Detailed technical specifications