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Literature summary for 3.4.23.5 extracted from

  • Buckow, R.; Truong, B.; Versteeg, C.
    Bovine cathepsin D activity under high pressure (2010), Food Chem., 120, 474-481.
    View publication on PubMed

General Stability

General Stability Organism
the protease is largely pressure stable at room temperature. At 100 MPa a significant stabilisation of the enzyme against temperature-induced inactivation is observed. Pressure drastically inhibits the cleavage by cathepsin D in Bis-Tris buffer (pH 6.0) causing a reduction of the catalytic rate of more than 50% at 100-400 MPa. The enzyme is relatively stable with more than 57% and 40% residual activity after 30 min treatment at 30°C and 300 MPa or 400 MPa, respectively. At higher pressures the enzyme is destabilised rapidly resulting in a residual activity of less than 10% after 30 min treatment at 600 MPa Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
spleen
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hemoglobin + H2O
-
Bos taurus ?
-
?
Myoglobin + H2O the hydrolysis rate is fairly slow Bos taurus ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
maximal substrate cleavage by cathepsin D is identified at 60°C and ambient pressure conditions after 20 min treatment Bos taurus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 60 the protease is heat stable at ambient pressure up to 300 MPa and 55°C, respectively, causing less than 10% inactivation after 10 min treatment. Cathepsin D is quickly inactivated at temperatures above 60°C Bos taurus