INFLUENCE OF ADDITION OF K + METAL ION (IN FORM
KHPO4 COMPOUND) TO ENZYME TRIPSIN ACTIVITY.
S1 thesis, Faculty of Mathematics and Natural Sciences UNY.
This study aims to determine the effect of adding K + metal ions
in the form of KHPO4 compound on the activity of trypsin enzyme. Previous
the optimum conditions of trypsin enzyme include pH, temperature, incubation time, and
substrate concentration. The subject of this research is trypsin enzyme activity with
the object of trypsin enzyme activity with the addition of K + inner metal ions
form of KHPO4 compound in various concentration variations, ie 0.01 M; 0.03 M;
0.05 M; 0.07 M; and 0.09 M. Protein content was determined using the method
Lowry. The activity of trypsin enzyme is determined by Anson method. Determination
the activity of trypsin enzyme with casein substrate was done at optimum condition.
The data obtained is the activity of trypsin enzyme in units of mg / mL / min.
The data analysis used is descriptive qualitative, so it can be known
the role of metal ions in the form of activators or inhibitors. The results showed
trypsin enzyme protein levels of 0.074 mg / mL. Optimum condition of trypsin enzyme
at pH 8, 37 ° C, 20 min incubation time, and substrate concentration of 10
mg / mL. The activity of trypsin enzyme is 0.00312 mg / mL / min. Enzyme activity
trypsin with the addition of K + metal ions at a concentration of 0.01 M; 0.03 M; 0.05
M; 0.07 M; and 0.09 M and 37 ° C respectively of 0.00320; 0.00337;
0.00360; 0.00375 mg / mL; and 0.00427 mg / mL / min. Therefore,
the addition of K + metal ions in the form of a KHPO4 compound is an activator
to the activity of trypsin enzyme under optimum conditions.
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