CD Skripsi

Pengaruh Penambahan Edta, Sodium Azida, Urea, Sds Dan Triton X-100 Terhadap Aktivitas Enzim Lakase A dan B Trichoderma Asperellum Lbkurcc1

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Laccase enzyme is an extracellular enzyme that can catalyze the lignin degradation process, and degradation of textile dyes by oxidation. The advantages of using the laccase enzyme is because the laccase enzyme oxidizes the substrate without H2O2 so this enzyme is more environmentally friendly. This research used laccase enzymes A and B obtained from the fungi Trichoderma asperellum LBKURCC1. Laccase was semipurified from its crude extract by 0-80% ammonium sulfate presipitation, followed by gel filtration column chromatography. The aim of this research was to analyze the effect of adding EDTA, sodium azide, urea, SDS and triton X-100 compounds on the activity of the laccase enzyme with variation concentrations of 1 mM and 10 mM. Laccase enzyme activity was determined by using 2,2'-azinobis-3-ethylbenzothiazoline-6-sulfonate (ABTS) as substrate. Changes in the visible light absorption due to oxidation of ABTS catalyzed by laccase was measured at a wavelength of 420 nm using a UV-Vis spectrophotometer with incubation times of 0 minutes and 5 minutes. The laccase enzyme used in this research has an optimum temperature of 45C and an optimum pH of 5,5 with an average activity of A and B respectively of 163,045,43 U/L and 144,022,71 U/L. The results of this study showed that the addition of all additives was able to significantly reduce the activity of laccase A and B, except for the addition of EDTA with a concentration of 1 mM and urea with a concentration of 1 mM based on t test (p0,05). The addition of urea with a concentrantion of 10 mM act as activators both for laccase A and B, which increased becoming (1268)% of the control activity for laccase A and becoming (1314)% of the control activity for laccase B. In laccase A, the highest decrease in laccase activity occurred with the addition of 10 mM triton X-100, which decreased to become only (206)% of the laccase control activity. In laccase B, the highest decrease in laccase activity occurred with the addition of 10 mM SDS, becoming only (91)% of the laccase control activity.

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Ketersediaan

Informasi Detail

Judul Seri

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No. Panggil

1803124033

Penerbit

Pekanbaru : Universitas Riau – FMIPA - Kimia., 2023

Deskripsi Fisik

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Bahasa

Indonesia

ISBN/ISSN

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Klasifikasi

1803124033

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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