pH-Spectrum of
the catabolism of Gelatine by
the enzyme Trypsin



recorded by Dr. G. Mermigidis

Experimental:

System (G+T) - (40 mg/L Trypsin / 0.1 % solution of Gelatine),
System (IS05/1+T)` - (12/24 mg/L Soybean inhibitor + 40 mg/L Trypsin / 0.1 % solution of Gelatine),
System (G+5T) - (200 mg/L Trypsin / 0.2 % solution of Gelatine),
System (IS05/1+5T)` - (60/180 mg/L Soybean inhibitor + 200 mg/L Trypsin / 0.2 % solution of Gelatine),
System G - (0.2 % solution of Gelatine),
System 5T - (200 mg/L Trypsin / dist. water),
System (G+5T)` - (200 mg/L Trypsin / 0.4 % solution of Gelatine)


Results:

Fingerprints

System G/5T: The consume of H+/OH--ions by Gelatine/Trypsin.

Systemprints

System (G+T/G+5T): Shows the interaction between Gelatine and Trypsin at pH 4.5 to 9. The surplus of OH--ions is at pH 8.4 like the quantity of Trypsin one/five fold. The catabolism of Gelatine by Trypsin coud be shown by the consume of H+-ions, it is at pH 2 like the quantity of Gelatine one/two fold.

Systemprints with Additive, helps you to check the influence of an Additive

System (IS05/1+T and IS05/1+5T)`: The consume of H+-ions at pH 2 have been reduce to 50%/100% by the addition of Soybean inhibitor.
System (G+5T)`: Both peaks at pH 4/8.3 are equivalent to the activity-area of the enzyme Trypsin, the point of Vmax is at pH 8.3.

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