Affiliation:
1. Department of Chemistry, Faculty of Mathematics and Natural Sciences University of Lampung, Bandar Lampung-35145, Indonesia.
Abstract
The thermal stability increase of a-amylase obtained from locale bacteria isolate Bacillus subtilis ITBCCB148 was achieved by immobilization process using an ionic exchange matrix of DEAE-Cellulose. The result showed that the immobilized enzyme has an optimum temperature of 60°C; KM 14.8 mL substrate and Vmax 42.4 U/mL. The thermal stability storage temperature of 60°C, pH 9.0 and 60 minutes demonstrated the immobilized enzyme has residual activity of 28.1%; ki = 0.0224 min.-1; and ΔGi = 103.7 kJ mol-1. Although the immobilized enzyme’s thermal stability was only increased 1.5 times, at higher temperatures, it was much more stable than the native enzyme.
Publisher
Oriental Scientific Publishing Company
Subject
Pharmacology (medical),Complementary and alternative medicine,Pharmaceutical Science
Cited by
3 articles.
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