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Potensi Lakase Dari Trichoderma Asperellum Lbkurcc1 Dalam Biodegradasi Antibiotik Amoxicillin
Laccase enzyme (E.C1.10.3.2: oxygen oxidoreductase) is a multi-copper enzyme that catalyzes the oxidation process of various types of organic and inorganic compounds such as mono, di- and polyphenol compounds, aminophenols, methoxyphenols, substituted phenols, diamines, aromatic amines and ascorbic acid. Laccase is an oxidoreductase enzyme produced by various organisms, primarily fungi. This research used laccase enzyme A obtained from the fungi Trichoderma asperellum LBKURCC1. Laccase enzyme from this isolate has been previously employed in several studies for the degradation of textile dyes. The aim of this research was to analyze the potential of the laccase enzyme in degrading the antibiotic amoxicillin. The laccase enzyme activity was measured using ABTS (2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid)) as the substrate. The change in absorbance of the substrate, caused by the oxidation reaction catalyzed by laccase, was monitored using a microplate reader at 405 nm wavelenght with an incubation time of 0 minutes and 5 minutes. The laccase enzyme A activity obtained was approximately 118.546±1.109 U/L. The degradation process used two types of enzyme concentration, 25 U and 50 U, at three different pH levels: 4.5, 5.5 and 6.5. Measurements were taken by using a UV-Vis spectrophotometer to observe the decrease in absorbance over several days. The results showed a significant reduction in absorbance at pH 5.5 and 50 U of laccase enzyme concentration was used. At this pH and enzyme concentration, the degradation percentage was found to be 29.89±1.794%. This indicates that the laccase enzyme from the Trichoderma sp. LBKURCC1 fungus exhibits optimal enzyme activity at pH 5.5.
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