CD Skripsi

Potensi Lakase Dari Trichoderma Asperellum Lbkurcc1 Dalam Biodegradasi Antibiotik Chloramphenicol

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Laccase (benzenediol: oxygen oxidoreductase, EC 1.10.3.2) is a p-diphenol: dioxygen oxidoreductase classified as a multi-copper protein and has broad substrate specificity. The potential of laccase as one of the enzymes produced from fungal isolate Trichoderma asperellum LBKURCC1 has been reported in the enzymatic degradation of several chemical compounds such as synthetic dyes. This research focused on on utilizing laccase from a local isolate of the fungus Trichoderma asperellum LBKURCC1 to degrade the antibiotic Chloramphenicol. Chloramphenicol is a broad-spectrum antibiotic poses a significant environmental threat due to improper use and disposal, posing a threat to human health and the environment. This research aimed to investigate the activity of laccase A produced by Trichoderma asperellum at its optimal pH and assess its effectiveness in degrading Chloramphenicol. Enzyme activity was measured using ABTS as substrate, and Chloramphenicol degradation by laccase was monitored with UV-Vis spectrophotometry. The study was conducted at two enzyme concentrations (25 U/L and 50 U/L) and various pH levels (4.5, 5.5, and 6.5). Laccase A exhibited an activity of 118.546 U/L and showed potential for bioremediation of pharmaceuticals like Chloramphenicol. The results were quite promising, with the optimal conditions for Chloramphenicol degradation by laccase A being an enzyme concentration of 50 U/L, pH 4.5 and a reaction time of 5 days. Under these conditions, laccase A reduced the antibiotic concentration by 32.3%. 

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Ketersediaan

Informasi Detail

Judul Seri

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No. Panggil

2003113837

Penerbit

Pekanbaru : Universitas Riau FMIPA Kimia., 2024

Deskripsi Fisik

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Bahasa

Indonesia

ISBN/ISSN

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Klasifikasi

2003113837

Tipe Isi

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Tipe Media

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Tipe Pembawa

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Edisi

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Subjek

KIMIA

Info Detail Spesifik

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Pernyataan Tanggungjawab

Mutia

Versi lain/terkait

Lampiran Berkas

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