Trypsin is a serine protease derived from pancreas. It is a single chain polypeptide of 223 amino acid residues with substrate specificity based on positively charged Lysine and Arginine side chains. Trypsin predominantly cleaves peptide chains at the carboxyl side of Lysine and Arginine, except when either is followed by Proline. Trypsin is produced from Trypsinogen by removal of a terminal hexapeptide to yield a single chain native form of trypsin called β-Trypsin. Subsequent autolysis of β-Trypsin results in α-Trypsin having two peptide chains bound by disulphide bonds.
Activity
Optimum pH for trypsin activity
7.0-9.0
Optimum temperature
37°C
BAEE unit definition
One BAEE unit will produce a ΔA253nm of 0.001 per minute with BAEE as substrate at pH 7.6 at 25°C in a reaction volume of 3.2ml (1cm light path).
TAME unit definition
One TAME unit hydrolyzes 1µmole of p-toluene-sulfonyl-L-arginine methyl ester (TAME) per minute at 25°C, pH 8.2 in the presence of 0.001M calcium ion.
USP trypsin unit definition
One USP trypsin unit is the activity causing a change in absorbance of 0.003 per minute under the conditions specified.
Activity Conversion
1 TAME unit = 19.2 USP or NF units= 57.5 BAEE Units.
Quality Control
Appearance
White to yellow crystals or powder
Solubility
33.3 mg soluble in 1 mL of water
Activity (on dry basis)
NLT 2500 USP U/mg
Unit definition (BAEE)
One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25°C using BAEE as substrate. Reaction volume = 3.2 ml (1 cm light path)
Cell Culture Test
Passes
Storage and Shelf Life
Storage conditions
Store at 2-8°C away from bright light.
Reconstituted storage
Trypsin after reconstitution should be stored at -20°C.
Usage
Use before expiry date given on the product label.