Detail Partial purification of Trichoderma asperellum LBKURCC1 laccase by ammonium sulfate fractionation and ultrafiltration dialysis (article of AIP Conference Proceedings, Volume 2480, Issue 1, id.040011, 7 pp. May 2023) Bibliografi Author: Dahliaty, Andi ; Amalita, Lisna ; Putri, Yorin P. ; Ristanti, Wanda A. ; Yanti ; Nugroho, Titania Tjandrawati Bahasa: (EN )     Penerbit: AIP Publishing     Tahun Terbit: 2023     Jenis: Article - diterbitkan dalam Proceeding Internasional Fulltext: Partial purification of Trichoderma asperellum LBKURCC1.pdf (1,021.55KB; 2 download) Abstract Laccase is an important enzyme for industry, due to its many biotechnological applications, among others degradation of dyes from textile waste effluents, synthesis of fine chemicals and synthesis of eco-friendly cosmetic colors. Trichoderma asperellum LBKURCC1 is a biocontrol fungal strain that was isolated from Riau soil, that can produce laccase in a Solid-State Fermentation (SSF) system using rice straw as laccase inducer. Crude laccase enzyme extracts from the rice straw SSF system contain also tannic acid compounds. The aim of this researchwasthe partial purification of T. asperellum LBKURCC1 laccase by ammonium sulfate salting-out fractionation, followed by ultrafiltration dialysis. Fractionation was done by successive precipitation of the enzyme with the addition of solid ammonium sulfate to crude enzyme solution until various salt saturation. The resulting precipitate was dissolved in buffer and dialyzed using ultrafiltration (UF) centrifugation with 10 kDa and 50 kDa Molecular Weight Cut Off (MWCO) polyethersulfone (PES) membranes. Laccase activity was determined based on the assay using 2,2'-azino-bis (3-ethylbenzothiazholine-6-sulphonic acid) (ABTS) as laccase substrate. The results showed that dialysis and repeated washing of the precipitate using 10 kDa MWCOUF membranes could not eliminate completely tannic compounds that interfered with the laccase activity assay. Subsequent dialysis using 50 kDa UF membranes succeeded in elimination of tannic compounds from the enzyme preparation. Highest activity of laccase was found at the 20-40% saturated ammonium sulfate fraction, with an increase in specific activity by 2.5 times compared to its specific activity in the crude enzyme extract. The specific activity of the 20- 40% saturated ammonium sulfate fraction was 0.33 U/mg protein, with a 13% yield. Another fraction, 40-60% saturated ammonium sulfate fraction, also gave an increase in specific activity compared to crude extracts, but only 1.7 times and 10% yield. These results show that partial purification of laccase has been achieved. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Lihat Sejarah Pengadaan  Konversi Metadata   Kembali

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