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KI 6161 – ENZIMOLOGI Laccase : Sifat dan Aplikasinya

KI 6161 – ENZIMOLOGI Laccase : Sifat dan Aplikasinya. Aisyah ( 10509057) Bunga Annisa (10509089). Agenda Presentasi. Struktur & Sifat Molekular Laccase (EC 1.10.3.2) . Enzim oksidoreduktase yang bekerja pada substrat difenol sebagai donor

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KI 6161 – ENZIMOLOGI Laccase : Sifat dan Aplikasinya

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  1. KI 6161 – ENZIMOLOGILaccase: SifatdanAplikasinya Aisyah (10509057) BungaAnnisa (10509089)

  2. Agenda Presentasi

  3. Struktur& SifatMolekularLaccase(EC 1.10.3.2) • Enzimoksidoreduktase yang bekerjapadasubstratdifenolsebagaidonor • Memilikigugus 1,4-benzendiol dan 4 atom tembaga per monomer • Cu tipe 1  tempatsubstrattereduksi • Cu tipe 2 & 3  pusattrinuklir yang mengikatoksigen

  4. MekanismekatalisisLaccase • Katalisissubstrat non-fenolik: • Bantuanmediator • HOBT, NHPI, ABTS dan3-asam hidroksianthranilik

  5. SumberLaccase

  6. IsolasidanPemurnianLaccase

  7. ProduksiLaccase

  8. ProduksiLaccase (Cont)

  9. Kinetika • Penentuanmengukurlajupembentukansubstratteroksidasi • Bergantungterhadapjenissubstrat • Contoh : • Trameteshirsutadengansubstrat ABTS • ABTS teroksidasidiukurjumlahnyamenggunakanspektrofotometer.

  10. Faktor yang mempengaruhiaktivitasLaccase Kinetika (Cont.)

  11. Modifikasi

  12. Modifikasi(Cont) Perbandingan parameter kinetikaFree LaccasedanImmobilized Laccase

  13. Modifikasi (Cont.)

  14. PeranLaccase

  15. PeranLaccase (Cont)

  16. Dapus • Shraddha, Ravi Shekher, SimranSehgal,MohitKamthania, and Ajay Kumar. Laccase:Microbial Sources, Production, Purification, and Potential Biotechnological Applications. 2011. Enzyme Research, Article ID 217861, pp 1-11 • Madhavi, Vernekar. Laccase: Properties and Application. 2009. BioResources 4(4). Pp 1694-1717 • Sunil S.More, Renuka P. S, Pruthvi K., SwethaM., S.Malini, and Veena S. M. Isolation, Purification, and Characterization of Fungal LaccasefromPleurotus sp. 2009. Enzyme Research. Article ID 248735, pp 1-7 • Schroeder, M. et.al., Specificities of a chemically modified laccase from Trameteshirsuta on soluble and cellulose-bound substrates. Biotechnology Letters. 2006, Volume 28, Issue 10, pp 741-74 • C, Galli.,et,all. How is the reactivity of laccase affected by single-point mutations? Engineering laccase for improved activity towards sterically demanding substrates. ApplMicrobiolBiotechnol.2011. Epub 2011. p:123-31.

  17. TerimaKasih

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