<![CDATA[Protease enzymes such as bromelain from Ananas comosus and papain from Carica papaya are cysteine protease enzymes that have great potential in various applications in the food, pharmaceutical, and biotechnology industries. This study aims to characterize the activity of bromelain and papain enzymes against pH variations using a casein-based spectrophotometric method and a tyrosine standard curve. Enzyme activity is determined based on the amount of tyrosine produced from casein hydrolysis and measured at a wavelength of 280 nm. One unit of enzyme activity is defined as the amount of enzyme that produces 1 µmol of tyrosine per mL per unit reaction time. The yields of bromelain and papain enzyme extraction in this study reached 38% and 32% with protein levels of 10.04 and 21.89 mg/mL, respectively. The activity values of bromelain and papain are significantly affected by changes in pH. Bromelain showed optimum activity at pH 6, amounting to 25.4 U/mL, while the activity decreased drastically at acidic pH. The papain enzyme also has an optimum activity of 17.1 U/mL at pH 6, which decreases drastically at alkaline pH. This activity pattern is consistent with the general characteristics of cysteine protease enzymes, which are sensitive to changes in the ionization of their active groups. The differences in response to pH variations indicate the specific characteristics of each enzyme, influenced by the structure and conformational stability of its protein. The results of this study provide important information regarding the optimum working conditions of both enzymes as a basis for developing industrial applications based on local biological resources.]]>
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