For Enzymatic Hydrolysis of Protein CAS 9002-07-7 Recombinant
Enzyme Commission (EC) Number: 220.127.116.11
Molecular Weight: 23.3 kDa (bovine & porcine)
Extinction Coefficient: E1% = 12.9 - 15.4 (280 nm)
pI: 10.1 - 10.5
Trypsin is a member of the serine protease family. Trypsin cleaves
peptides on the C-terminal
end of lysine and arginine amino acid residues. The optimum pH of
trypsin is pH 7 - 10. The
enzyme is inhibited by serine protease inhibitors, e.g. PMSF and by
metal chelating agents,
e.g.EDTA.Trypsin will cleave peptides on the C-terminal side of
lysine and arginine amino acid
residues. The rate of hydrolysis is slower if an acidic residue is
on either side of the cleavage
site and no cleavage occurs if a proline residue is on the carboxyl
side of the cleavage site.
Trypsin will hydrolyze ester and amide linkages of several
Recombinant Porcine Trypsin is a genetically engineered protein
expressed in E.coli and purified
by high pressure liquid chromatography. There are no contaminating
enzyme activities such as carboxypeptidase A and chymotrypsin. No
protease inhibitors such as PMSF are contained in the preparation.
The activity of most preparations is determined by a continuous
rate spectrophotometric assay
and expressed in BAEE units.
Unit Definition: 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).
Prepare 1-10mg/ml recombinant trypsin with 1mM HCl.The ratio to
aimed protein is 1:50 to 1:1000 (w/w).The optimum pH is pH7-10.
Recombinant trypsin lyophilized should be stored under 2℃-8℃ in
sealed container. It is stable
within 24 months.After dissolved, it should be stored under -20℃.
It is stable within 24 months
and above 90% activity remained after 10 times repeated freezing