MEDALIYANA OKTAVIA, - (2022) Characterization of Protease Enzyme from Bacterial Isolate EKA 20 Endosymbionts of Cockroach Pycnoscelus surinamensis. Skripsi thesis, UNIVERSITAS AIRLANGGA.

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Abstract

This study aims to determine the characterization of protease enzymes from bacterial isolate EKA 20 endosymbionts of the cockroach Pycnoscelus surinamensis, by testing variations in temperature, pH, and addition of several types of metal ions. Enzyme activity was tested using the Bergmeyer & Grassl method (1983) while the protein content of the enzyme was tested using the Lowry method. The protease enzyme produced for 24 hours had an average enzyme activity value of 0.053 U/mL with a protein content of 4.651 mg/mL and a specific enzyme activity of 0.011 U/mg. The protease enzyme from bacterial isolate EKA 20 had a protease index (IP) of 3 for 24 hours of incubation. The results showed that variations in temperature, pH, and the addition of metal ions affected the protease enzyme activity of the bacterial isolate EKA 20.The highest protease enzyme activity was at 60?C with a value of 0.064U/mL. The highest enzyme activity at pH variation was found at pH 5, which was 0.058 U/mL. The highest protease enzyme activity was obtained at the interaction treatment at 60?C and pH 5, which was 0.058 U/mL, while the lowest protease activity was obtained at the interaction treatment at 60?C and pH 7, which was 0.044 U/mL. The addition of metal ions Mg2+ and Fe2+ in the protease enzyme activity test functioned as activators while metal ions Ca2+, Cu2+, and Mn2+ functioned as inhibitors.

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