IMMOBILIZATION OF ?-AMYLASE ENZYME ON POLY METHYL METHACRYLATE (PMMA) MATRIX

• Main Author: Wiradinata M, Arbi
• Format: Final Project
• Language: Indonesia
• Subjects: Kimia
• Online Access: https://digilib.itb.ac.id/gdl/view/35136
• Institution: Institut Teknologi Bandung

Activation of poly(methyl methacrylate) (PMMA) is needed to enable the formation of covalent bonds between PMMA and enzymes. In this study, PMMA has been activated using NaOH, H2SO4, and H2SO4- ethylenediamine. Activation with NaOH showed negative result because there was no change in FTIR spectrum before and after activation. Activation was successfully carried out using a 12 M H2SO4 solution at 60? for 2 hours which is indicated by the appearance of a new peak at wavenumber 3401 cm-1 which is identified as the presence of hydroxyl group formed after activation with H2SO4. Activation of H2SO4- ethylenediamine was carried out by reacting ethylenediamine at 60? for 2 hours with PMMA which had been activated by H2SO4 before. This activation technique also gives a positive result which is indicated by the vibration of the primary amine group at wavenumber 3003 and 1479 cm-1. The immobilization of alpha amylase on both activated PMMA surfaces was successfully carried out. Testing of enzyme activity against a 0.1% starch substrate in acetate buffer 0.1 M pH 5 and contact time of 30 minutes showed the presence of reducing sugars produced. In this test, PMMA matrix which has been activated by H2SO4 gives the best results (approx. 50% of free enzyme activity), so repeated usage testing is carried out on this immobilized enzyme. Repetition of three times gave the reducing sugar concentration respectively 935,94 ppm; 444,78 ppm; and 232,27 ppm. SEM photos also convince that alpha amylase has been immobilized on the activated PMMA surface. In the morphological photo of the surface with magnification to 10,000 times, there is an enzyme attached to the surface of PMMA and the enzyme that is released after use to starch.