| Size | Price | Stock | Qty |
|---|---|---|---|
| 10g |
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| 25g |
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| 50g |
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| Other Sizes |
| Targets |
Proteins and peptide substrates (aspartic endopeptidase). Aspergillopepsin I is an aspartic endopeptidase that catalyzes the hydrolysis of peptide bonds in proteins. The enzyme has broad substrate specificity, generally favoring hydrophobic residues in the P1 and P1' positions, but also accepts lysine in P1, which leads to activation of trypsinogen. As an aspartic protease, it contains two conserved aspartic acid residues in the active site that are essential for catalytic activity. The enzyme does not clot milk.
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| ln Vitro |
Aspergillopepsin I exhibits high catalytic activity and stability under acidic conditions. The enzyme has broad substrate specificity, hydrolyzing peptide bonds in proteins with efficient proteolysis. It generally favors hydrophobic residues in the P1 and P1' positions but also accepts lysine in P1. The enzyme's activity can be measured using various protein substrates, and its stability under different pH and temperature conditions has been characterized. It is used in research to generate peptide fragments for analytical purposes.
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| ln Vivo |
In vivo studies of aspergillopepsin I are limited as it is primarily used as an in vitro research tool and industrial enzyme. The enzyme is not administered systemically for therapeutic purposes. Its applications are focused on protein hydrolysis in laboratory and industrial settings. The enzyme's stability and activity under various conditions make it suitable for use in food processing, protein digestion studies, and peptide mapping.
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| Enzyme Assay |
Non-cell-based assays for aspergillopepsin I involve protease activity measurements using protein substrates such as casein, hemoglobin, or synthetic peptide substrates. The enzyme is incubated with substrate at acidic pH (typically pH 2-4), and proteolytic activity is measured by monitoring the release of amino acids or peptide fragments using spectrophotometric methods (e.g., Folin-Ciocalteu reagent) or HPLC. The effect of inhibitors (e.g., pepstatin A) can be assessed to confirm aspartic protease activity. Enzyme stability is evaluated under various pH and temperature conditions.
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| Cell Assay |
Cell-based assays for aspergillopepsin I are not commonly performed, as the enzyme is primarily used for in vitro protein hydrolysis rather than cell-based studies. In research applications, the enzyme may be used to generate peptide fragments from cellular proteins for downstream analysis such as mass spectrometry or peptide mapping. Cytotoxicity of the enzyme is not typically assessed as it is not used in cell culture applications.
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| Animal Protocol |
In vivo animal studies for aspergillopepsin I are not applicable as the enzyme is not administered as a therapeutic agent. It is used exclusively as a research tool and industrial enzyme for in vitro protein hydrolysis. Studies on the enzyme focus on its biochemical properties, substrate specificity, and stability rather than in vivo effects.
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| ADME/Pharmacokinetics |
Aspergillopepsin I has a CAS number of 9025-49-4 and is classified under EC 3.4.23.18. The enzyme appears as a light brown to brown solid powder with a density of 1.3±0.1 g/cm³. It is produced by Aspergillus niger and is also known by various synonyms including Aspergillus acid protease, Protease, Acidic Protease, Proteinase, pepA, aspergillopepsin A, aspergillopepsin F, aspergillopeptidase A, awamorin, proctase B, and trypsinogen kinase. The enzyme should be stored under recommended conditions as specified in the certificate of analysis.
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| Toxicity/Toxicokinetics |
Aspergillopepsin I is generally considered safe for research and industrial applications. As an enzyme derived from Aspergillus niger, it is widely used in food processing and has a history of safe use. However, appropriate safety precautions should be taken when handling the enzyme powder, including the use of personal protective equipment to avoid inhalation or skin contact. The enzyme is not intended for therapeutic use.
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| References |
[1]. Lambré C, et al. Safety evaluation of a food enzyme containing aspergillopepsin I and II from the Aspergillus niger var. macrosporus strain PTG8398. EFSA J. 2022 Aug 11;20(8):e07471.
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| Additional Infomation |
Aspergillopepsin I (Aspergillus acid protease) is an aspartic endopeptidase that catalyzes the hydrolysis of peptide bonds in proteins with broad specificity. It is classified under EC 3.4.23.18 and is produced by Aspergillus species, particularly Aspergillus niger. The enzyme generally favors hydrophobic residues in the P1 and P1' positions but also accepts lysine in P1, which leads to activation of trypsinogen. Aspergillopepsin I exhibits high catalytic activity and stability under acidic conditions, making it valuable for industrial applications requiring precise proteolysis. It is also used in research to study protein structure-function relationships and to generate peptide fragments for analytical purposes. The enzyme is for research use only.
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| Exact Mass |
232.084
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|---|---|
| CAS # |
9025-49-4
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| PubChem CID |
168009823
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| Appearance |
Light brown to brown solid powder
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| Density |
1.3±0.1 g/cm3
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| Boiling Point |
413.1±45.0 °C at 760 mmHg
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| Flash Point |
203.6±28.7 °C
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| Vapour Pressure |
0.0±1.0 mmHg at 25°C
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| Index of Refraction |
1.605
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| LogP |
1.19
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| Hydrogen Bond Donor Count |
4
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| Hydrogen Bond Acceptor Count |
34
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| Rotatable Bond Count |
49
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| Heavy Atom Count |
103
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| Complexity |
2190
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| Defined Atom Stereocenter Count |
0
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| SMILES |
CC1=C(OC(=C)O1)COC(=O)C(C(C)(C)COC(=O)C=CC(=O)OC)O.CC(C)C(=O)OCOC(=O)C(C(C)(C)COC(=O)C=CC(=O)OC)O.CC(C)(COC(=O)C=CC(=O)OC)C(C(=O)OCCCN1C=CN=C1)O.CC(C)(COC(=O)C=CC(=O)OC)C(C(=O)OCCN1CCCCC1)O
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| InChi Key |
RUWHAENIXFIHPU-UHFFFAOYSA-N
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| InChi Code |
InChI=1S/C18H29NO7.C17H24N2O7.C17H22O9.C16H24O9/c1-18(2,13-26-15(21)8-7-14(20)24-3)16(22)17(23)25-12-11-19-9-5-4-6-10-19;1-17(2,11-26-14(21)6-5-13(20)24-3)15(22)16(23)25-10-4-8-19-9-7-18-12-19;1-10-12(26-11(2)25-10)8-23-16(21)15(20)17(3,4)9-24-14(19)7-6-13(18)22-5;1-10(2)14(20)24-9-25-15(21)13(19)16(3,4)8-23-12(18)7-6-11(17)22-5/h7-8,16,22H,4-6,9-13H2,1-3H3;5-7,9,12,15,22H,4,8,10-11H2,1-3H3;6-7,15,20H,2,8-9H2,1,3-5H3;6-7,10,13,19H,8-9H2,1-5H3
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| Chemical Name |
4-O-[3-hydroxy-2,2-dimethyl-4-[(5-methyl-2-methylidene-1,3-dioxol-4-yl)methoxy]-4-oxobutyl] 1-O-methyl but-2-enedioate;4-O-[3-hydroxy-2,2-dimethyl-4-(2-methylpropanoyloxymethoxy)-4-oxobutyl] 1-O-methyl but-2-enedioate;4-O-[3-hydroxy-2,2-dimethyl-4-oxo-4-(2-piperidin-1-ylethoxy)butyl] 1-O-methyl but-2-enedioate;4-O-[3-hydroxy-4-(3-imidazol-1-ylpropoxy)-2,2-dimethyl-4-oxobutyl] 1-O-methyl but-2-enedioate
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| HS Tariff Code |
2934.99.9001
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| Storage |
Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month |
| Shipping Condition |
Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)
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| Solubility (In Vitro) |
May dissolve in DMSO (in most cases), if not, try other solvents such as H2O, Ethanol, or DMF with a minute amount of products to avoid loss of samples
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| Solubility (In Vivo) |
Note: Listed below are some common formulations that may be used to formulate products with low water solubility (e.g. < 1 mg/mL), you may test these formulations using a minute amount of products to avoid loss of samples.
Injection Formulations
Injection Formulation 1: DMSO : Tween 80： Saline = 10 : 5 : 85 (i.e. 100 μL DMSO stock solution → 50 μL Tween 80 → 850 μL Saline)(e.g. IP/IV/IM/SC) *Preparation of saline: Dissolve 0.9 g of sodium chloride in 100 mL ddH ₂ O to obtain a clear solution. Injection Formulation 2: DMSO : PEG300 ：Tween 80 : Saline = 10 : 40 : 5 : 45 (i.e. 100 μL DMSO → 400 μLPEG300 → 50 μL Tween 80 → 450 μL Saline) Injection Formulation 3: DMSO : Corn oil = 10 : 90 (i.e. 100 μL DMSO → 900 μL Corn oil) Example: Take the Injection Formulation 3 (DMSO : Corn oil = 10 : 90) as an example, if 1 mL of 2.5 mg/mL working solution is to be prepared, you can take 100 μL 25 mg/mL DMSO stock solution and add to 900 μL corn oil, mix well to obtain a clear or suspension solution (2.5 mg/mL, ready for use in animals). View More
Injection Formulation 4: DMSO : 20% SBE-β-CD in saline = 10 : 90 [i.e. 100 μL DMSO → 900 μL (20% SBE-β-CD in saline)] Oral Formulations
Oral Formulation 1: Suspend in 0.5% CMC Na (carboxymethylcellulose sodium) Oral Formulation 2: Suspend in 0.5% Carboxymethyl cellulose Example: Take the Oral Formulation 1 (Suspend in 0.5% CMC Na) as an example, if 100 mL of 2.5 mg/mL working solution is to be prepared, you can first prepare 0.5% CMC Na solution by measuring 0.5 g CMC Na and dissolve it in 100 mL ddH2O to obtain a clear solution; then add 250 mg of the product to 100 mL 0.5% CMC Na solution, to make the suspension solution (2.5 mg/mL, ready for use in animals). View More
Oral Formulation 3: Dissolved in PEG400 (Please use freshly prepared in vivo formulations for optimal results.) |
Calculation results
Working concentration： mg/mL；
Method for preparing DMSO stock solution： mg drug pre-dissolved in μL DMSO (stock solution concentration mg/mL). Please contact us first if the concentration exceeds the DMSO solubility of the batch of drug.
Method for preparing in vivo formulation:：Take μL DMSO stock solution, next add μL PEG300, mix and clarify, next addμL Tween 80, mix and clarify, next add μL ddH2O，mix and clarify.
(1) Please be sure that the solution is clear before the addition of next solvent. Dissolution methods like vortex, ultrasound or warming and heat may be used to aid dissolving.
(2) Be sure to add the solvent(s) in order.
Products are for research use only; We do not sell to patients
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