Trypsin

Base Information

• Chemical Name: Trypsin
• CAS No.: 9002-07-7
• Molecular Formula: Unspecified
• Molecular Weight: 372.1
• Hs Code.: 35079090
• Mol file: 9002-07-7.mol

Synonyms:Cocoonase;Pancreatic Trypsin Novo;Parenzyme;Parenzymol;Pseudotrypsin;Sperm receptor hydrolase;Tripcellim;Tryptar;Tryptec Formula One;Trypure;Trypzean;Typtar;

Chemical Property of Trypsin

Chemical Property:

• Appearance/Colour: white or whitish powder
• Vapor Pressure: 0Pa at 25℃
• Melting Point: 115°C
• PKA: pK1:6.25 (25°C,μ=0.1)
• PSA: 0.00000
• Density: 1.37[at 20℃]
• LogP: 0.00000
• Storage Temp.: −20°C
• Solubility.: Reconstitute in aqueous buffer
• Water Solubility.: Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml).

Purity/Quality:

99%, ^*data from raw suppliers

Trypsin 1:250 ^*data from reagent suppliers

Safty Information:

• Pictogram(s): R36/37/38:; R42:
• Hazard Codes: Xn,B
• Statements: 36/37/38-42-42/43
• Safety Statements: 22-24-26-36/37-45-23

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Description: Trypsin is a serine protease in the digestive system of human and animals. The main function of this enzyme is to hydrolyze proteins into smaller peptides or even amino acids. Trypsin and other digestive proteases such as chymotrypsin are responsible for the digestion of food protein in the small intestine. This proteolytic function of trypsin has been widely used in the protein chemistry, proteomics, and nutrition research. This function is influenced by the sources of enzyme, and environmental factors such as pH, temperature, and the presence of trypsin inhibitors in the enzymatic reaction medium. Trypsin is used in the food processing to improve the functional properties such as solubility, emulsification, foaming and gelling properties of food proteins, to improve the digestibility of vegetable and seed proteins. It is used to reduce the concentration of allergens in some foods and to produce protein hydrolysates and bioactive peptides that are used in infant formulas and for people with special health problems such as hypertension. In food science research, trypsin is used for the food protein sequencing, in-vitro determination of food protein digestibility.? In combination with bromelain and rutin, trypsin is used for osteoarthritis. Trypsin is used to remove necrotic tissue and debris during wound and ulcer cleaning. Trypsin supplements may be used to remove dead tissue cells that remain after trauma, infection or surgical procedures, allowing new skin or tissue cells to grow.
• Uses: Proteolytic enzyme. Trypsin is a digestive enzyme found in the digestive system. The enzyme catalyzes the hydrolysis of peptide bonds breaking down proteins into smaller peptides. Trypsin-EDTA Solution 10X has been used to release adherent cells from tissue culture plates for passaging.

Refernces

Enzymatic peptide synthesis with p-guanidinophenyl and p- (guanidinomethyl)phenyl esters as acyl donors

10.1248/cpb.46.846

The research focuses on the enzymatic peptide synthesis using "inverse substrates," specifically N-Boc-amino acid p-guanidinophenyl and p-(guanidinomethyl)phenyl esters, as acyl donor components. The purpose of the study was to analyze the kinetic behavior of these esters towards bovine and Streptomyces griseus (SG) trypsin and to discuss the spatial requirements of the active sites of these enzymes for catalytic efficiency based on the steric characteristics of the substrates. The research concluded that these substrates readily couple with amino acid p-nitroanilides to produce peptides, with SG trypsin being the most efficient catalyst among those tested. The study also highlighted the versatility of inverse substrates in peptide coupling reactions and the critical role of the acylation process in determining the coupling rate and yield. Key chemicals used in the process included N-Boc-amino acid derivatives, p-guanidinophenyl esters, p-(guanidinomethyl)phenyl esters, and various trypsin enzymes from different sources.

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