Browsing by Author "Nugroho, Titania T."

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    ANALISIS HASIL OKSIDASI BROMOCRESOL PURPLE OLEH LAKASE Trichoderma asperellum LBKURCC1 MENGGUNAKAN SPEKTROFOTOMETER FOURIER TRANSFORM INFRA RED
    (Elfitra, 2022-05) Wulandari, Nuria; Nugroho, Titania T.; Linggawati, Amilia
    Trichoderma asperellum LBKURCC1 is one of the biocontrol agents capable of producing the enzyme laccase. Laccase (EC 1.10.3.2) is an extracellular enzyme that contains copper ions and catalyzes the four-electron oxidation of various -OH containing substrates. T. asperellum LBKURCC1 laccase is able to oxidize several triphenylmethane textile dyes, including Bromocresol purple (BCP) dye. This study explores chemical changes of the dye, Bromocresol purple (BCP) by treatment with crude extracts of T. asperellum LBKURCC1 by analyzing its Fourier Transform Infra Red (FTIR) spectrum to determine changes in functional groups. The FTIR results did not show any addition or reduction of functional groups in BCP buffer controls, in BCP treated with the inactive enzyme, and with BCP treated with the active enzyme for 30 minutes and 6 days, respectively. However, there was a slight difference in the FTIR spectrum between 30 minutes and 6 days treatments, for all experiments, namely a decrease in the stretching of 2850 cm-1 due to the widening of the O-H stretching. This indicates that BCP is oxidized and leads to a more polar compound because the intensity of the O-H stretch increases and C-H which is a non-polar group decreases.
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    PENGARUH ION LOGAM Cu2+ DAN Mg2+ PADA AKTIVITAS LAKASE FRAKSI FLOW THROUGH KROMATOGRAFI GEL FILTRASI
    (Elfitra, 2023-11) Sinaga, Hana Hasanah; Nugroho, Titania T.; Dahliaty, Andi
    Laccase Trichoderma asperellum LBKURCC1 has been partially purified fractionation using ammonium sulfate at 0-80% saturation then gel filtration chromatography. The results of the gel filtration have different activities and purity levels The fraction has lower activity and lower purity is called laccase flow through gel filtration chromatography. The activity of the laccase enzyme was tested using substrates 2,2'-azinobis-3- ethylbenzothiazoline- 6-acid sulfonate (ABTS) measured at a wavelength of 405 nm using a microplate reader. The activity of laccase flow through is 144,02±2,71 U/L. The laccase activity was increased significantly (p≤ 0.05) to (362 ± 48)% and (445 ± 59)% compared to controls, when the enzyme was incubated for 10 minutes with 0.5 mM and 5 mM Cu2+ respectively. A significant increase (p≤ 0.05) in laccase activity was also observed when the enzyme was incubated for 10 minutes in 0.5 mM and 5 mM Mg2+, The laccase activity was increased significantly (p≤ 0.05) to (343 ± 59)% and (219 ± 50)% compared to controls.