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Literature summary for 3.4.21.4 extracted from

  • Venkatesh, R.; Sundaram, P.V.
    Modulation of stability properties of bovine trypsin after in vitro structural changes with a variety of chemical modifiers (1998), Protein Eng., 11, 691-698.
    View publication on PubMed

General Stability

General Stability Organism
no loss of activity upon modification up to 75-85% with monomeric glutaraldehyde, polymeric glutaraldehyde, oxidized sucrose and oxidized sucrose polymers. Modified trypsin resists exposure to 8 M urea in the presence and absence of 5 mM 2-mercaptoethanol, native enzyme loses its activity in 20 and 120 min Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.24
-
bovine serum albumin
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bovine serum albumin + H2O
-
Bos taurus ?
-
?
N-Benzoyl-L-Arg ethyl ester + H2O
-
Bos taurus ?
-
?
Nalpha-benzoyl-DL-Arg-p-nitroanilide + H2O
-
Bos taurus ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
native enzyme Bos taurus
55
-
enzyme modified with sucrose Bos taurus
60
-
enzyme modified with monomeric glutaraldehyde Bos taurus
68
-
enzyme modified with polymeric glutaraldehyde Bos taurus
74 76 enzyme modified with oxidized sucrose polymers Bos taurus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
half-life of native enzyme: 29.4 h Bos taurus
80
-
half-life of native enzyme: 126 s Bos taurus