Yandri, Yandri and Suhartati, Tati and Yuwono, Suripto D. and Qudus, Hardoko Insan and Tiarsa, E.R. and Hadi, Sutopo (2018) IMMOBILIZATION OF     -AMYLASE FROM BACILLUS SUBTILIS ITBCCB148 USING BENTONIT. Asian Journal of Microbiology, Biotechnology & Environmental Sciences, 20 (2). pp. 487-492. ISSN 0972-3005

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Abstract

This research aims to increase the stability of -amylase obtained from B. subtilis ITBCCB148 by immobilization process using bentonite matrix. The research phases performed were: production, isolation, purification, immobilization and characterization of purified and immobilized enzymes. The results showed that the purified -amylase had optimum temperature of 60oC, KM = 6.18 mg mL-1 substrate, and Vmax.= 909.09 mol mL-1 min.-1. The immobilized -amylase gave optimum temperature 75oC, KM = 12.19 mg mL1 substrate, and Vmax. = 88.50 mol mL-1 min.-1. The residual activities of the purified and immobilized enzymes on thermal stability test at 60°C for 100 minutes were 12 and 43%, respectively. The repetition used of the immobilized enzyme was 5 times. The thermodynamic data of the immobilized enzyme was t½ = 88.85 min., ki = 0.0078 min.-1, and Gi 106.65 kJ mol-1. Based on the decrease of ki and the increase of Gi and half-life (t½) the immobilization process with bentonite has successfully increase the stability of -amylase from B. subtilis ITBCCB148.

Item Type: Article
Uncontrolled Keywords:  -amylase, B. subtilis ITBCCB148, Bentonite, Immobilization
Subjects: Q Science > QD Chemistry
Divisions: Fakultas Matematika dan Ilmu Pengetahuan Alam (FMIPA) > Prodi Kimia
Depositing User: Prof. Sutopo Hadi
Date Deposited: 21 Jun 2018 01:51
Last Modified: 21 Jun 2018 01:51
URI: http://repository.lppm.unila.ac.id/id/eprint/7286

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