OPTIMIZATION OF KERATINASE ACTIVITY FROM BACILLUS LICHENIFORMIS

• Main Author: Cyntia
• Format: Final Project
• Language: Indonesia
• Subjects: Kimia
• Online Access: https://digilib.itb.ac.id/gdl/view/33669
• Institution: Institut Teknologi Bandung

Swallow nest has a huge potential in generating foreign exchange and become a mainstay of Indonesian exports. The price of swallow nest depends on the purity of the swallow nest. Impurities contained in the swallow nest that can affect the purity is feathers of swallow. Therefore it takes a series of stages in the production process that aims to degrade feathers contained in swallow nest without harming the swallow nest. Swallow feathers containing 80 to 90% protein. Proteins are composed of keratin which can be degraded by keratinase enzyme produced by Bacillus licheniformis. The medium used to culture B. licheniformis containing tryptone, as a source of nitrogen. Bacteria B. licheniformis in induction at a temperature of 370C by using a medium containing a few tryptone and substrate in the form of a feather to produce keratinase. Keratinase activity measured from the time of induction day 5 to day 9 to obtain the keratinase with an optimum activity. Measurement of enzyme activity carried out by Lowry method using Follin Ciocalteu reagent and tyrosine standard calibration curve. The measurement results showed keratinase activity with optimum activity was obtained on day 7. Keratinase on day 7 extracted and measured the activity of the variation of pH, enzyme concentration, and temperature to obtain the optimum working conditions keratinase. Optimization results show there are an optimum pH at pH 9,8, the optimum temperature at 310C, and 20% (%v/ v) enzyme concentration