Chymotrypsin

Base Information

• Chemical Name: Chymotrypsin
• CAS No.: 9004-07-3
• Molecular Formula: N/A
• Molecular Weight: 0
• Hs Code.: 35079090
• European Community (EC) Number: 232-671-2
• DSSTox Substance ID: DTXSID30988741
• NCI Thesaurus Code: C76568
• Mol file: 9004-07-3.mol

Synonyms:Alpha-Chymotrypsin Choay;Alphacutanée;Avazyme;Chymotrypsin

Chemical Property of Chymotrypsin

Chemical Property:

• Appearance/Colour: White crystallized powder
• Vapor Pressure: 0Pa at 25℃
• Melting Point: 127 ºC
• PSA: 0.00000
• Density: 1.37[at 20℃]
• LogP: 0.00000
• Storage Temp.: 2-8°C
• Solubility.: Reconstitute in 1mM HCl. Soluble at 10mg/ml in 1mM HCl. 2mM calc
• Water Solubility.: 125g/L at 25℃
• XLogP3: 0.4
• Hydrogen Bond Donor Count: 5
• Hydrogen Bond Acceptor Count: 8
• Rotatable Bond Count: 12
• Exact Mass: 499.17031277
• Heavy Atom Count: 36
• Complexity: 801

Purity/Quality:

99%, ^*data from raw suppliers

Chymotrypsin A ^*data from reagent suppliers

Safty Information:

• Hazard Codes: Xn,B
• Statements: 36/37/38-42/43-42
• Safety Statements: 26-36-36/37-24-22

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Canonical SMILES: C1=CC=C(C=C1)CC(C(=O)NC2=CC=C(C=C2)[N+](=O)[O-])NC(=O)CNC(=O)CNC(=O)CCC(=O)O
• General Description: Chymotrypsin is a protease enzyme that can be chemically modified to enhance its stability and efficiency in peptide synthesis, particularly in aqueous organic media. Studies have shown that modifications, such as acylation with water-soluble reagents, can improve its hydrolytic activity and peptide synthesis capability, even in high concentrations of organic solvents like DMF. For instance, chymotrypsin modified with a 20% benzyloxycarbonyl group demonstrated superior performance in catalyzing peptide bond formation under such conditions.

Refernces

Prediction of the solvent dependence of enzymatic prochiral selectivity by means of structure-based thermodynamic calculations

10.1021/ja952674t

The research aims to develop a quantitative model that predicts the solvent dependence of enzymatic selectivity based on the thermodynamics of substrate solvation. The study concludes that enzymatic prochiral selectivity in anhydrous organic solvents can be primarily attributed to changes in the relative solvation energies for the pro-R and pro-S binding modes of the substrate in the transition state. The model was found to perform well with crystalline enzymes, but not with amorphous enzyme powders due to their ill-defined structure. Key chemicals used in the process include γ-chymotrypsin, subtilisin Carlsberg, vinyl acetate, 2-(3,5-dimethoxybenzyl)-1,3-propanediol, and various organic solvents such as diisopropyl ether, cyclohexane, and acetonitrile, among others.

Characteristics of chymotrypsin modified with water-soluble acylating reagents and its peptide synthesis ability in aqueous organic media.

10.1271/bbb.56.441

The research discusses the characteristics of chymotrypsin, a protease enzyme, when modified with water-soluble acylating reagents, and its ability to synthesize peptides in aqueous organic media. The purpose of the study was to enhance the enzyme's stability and efficiency in peptide synthesis, particularly in the presence of organic solvents like N,N'-dimethylformamide (DMF). The researchers prepared several modified forms of chymotrypsin and compared their hydrolytic activity and peptide synthesis ability with the unmodified enzyme. They found that chymotrypsin modified with a 20% benzyloxycarbonyl group (Z(20)Csin) showed more favorable characteristics, including higher hydrolytic activity in aqueous DMF media and the ability to catalyze peptide bond formation in higher yields, even in 80% DMF media where hydrolytic reactions were not possible.