Inhibitors of Laccases: A Review

Couto, Susana Rodrı́guez; Herrera, Lidia

doi:10.2174/157340806778699262

Cited by 32 publications

(23 citation statements)

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“…Other chelators have also been shown to inhibit laccases, though the degree of sensitivity varies for individual enzymes. Halide ions can inhibit laccases by binding to the oxidized T2/T3 trinuclear copper center and preventing the reduction of oxygen to water (Couto and Toca, 2006). Insect MCOs follow this trend, being sensitive to azide, cyanide, and fluoride, but insensitive to chelators such as thiourea (and PTU), ( EDTA, 8-hydroxyquinoline, and o-phenanthroline (Table 4).…”

Section: Inhibition Of Insect Mcosmentioning

confidence: 98%

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Insect multicopper oxidases: Diversity, properties, and physiological roles

Dittmer

Kanost

2010

Insect Biochemistry and Molecular Biology

117

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Section: Inhibition Of Insect Mcosmentioning

confidence: 98%

“…With fungal laccases, cyanide, azide, and DETC are generally potent inhibitors (Baldrian, 2006;Couto and Toca, 2006). Other chelators have also been shown to inhibit laccases, though the degree of sensitivity varies for individual enzymes.…”

Section: Inhibition Of Insect Mcosmentioning

confidence: 99%

Insect multicopper oxidases: Diversity, properties, and physiological roles

Dittmer

Kanost

2010

Insect Biochemistry and Molecular Biology

117

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“…In contrast, Eggert et al (1996) reported that AA had no inhibitory effect on the Pycnoporus cinnabarinus and Coriolus hirsutus laccases. It is concluded that the effect of chelating agents on laccase stability varied among laccases from different microorganisms (Couto and Toca 2006b). Here, we observed negligible inhibitory effect of AA on the T. versicolor laccase even at high concentrations of AA (Fig.…”

Section: Resultsmentioning

confidence: 53%

Potential of acetylacetone as a mediator for Trametes versicolor laccase in enzymatic transformation of organic pollutants

Yang

Sun

Zhang

et al. 2015

Environ Sci Pollut Res

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Low-cost and environmentally friendly mediators could facilitate the application of laccase (EC 1.10.3.2) in variant biotechnological processes. Acetylacetone (AA) represents an inexpensive and low toxic small molecular diketone that has been proven as an effective mediator for laccase in free radical polymerization. However, the potential of AA as a mediator for laccase in pollutant detoxification and/or degradation is still unknown. In this work, the roles of AA in laccase-induced polymerization and transformation were investigated. AA was demonstrated to be a highly efficient mediator in the laccase-induced grafting copolymerization of acrylamide and chitosan. The efficacy of AA in the laccase-induced decoloration of malachite green (MG) was compared with that of the widely used 1-hydroxybenzotriazole (HBT). The laccase-AA system had the highest turnover number (TON, 39.1 μmol/U), followed by the laccase-only system (28.5 μmol/U), while the TON of the laccase-HBT system was the lowest (14.9 μmol/U). The pseudo-first-order transformation rate constant (k 1) of MG in the laccase-AA system was up to 0.283 h(-1) under the given conditions, while the k 1 of AA caused by laccase was only 0.008 h(-1). In the five-cycle run, the concentration of AA remained stable. The larger TON of the laccase-AA system and the stability of AA in the cycling runs demonstrate that AA was more recyclable than HBT in the LMS, leading to a prolonged serving life of laccase. These results suggest that AA might be a potential redox mediator for laccase.

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“…Kata kunci: Jamur pelapuk putih, enzim, isolat, Lac, MnP meningkatkan produksi etanol (Larsson, Cassland, & Jönsson, 2001), dan biosensor yaitu membantu mendeteksi beberapa senyawa fenol, oksigen, dan azida (Rodríguez Couto & Toca Herrera, 2006). Sementara enzim itu, MnP telah diaplikasikan lebih spesifik untuk kegiatan bioremediasi (Hidayat & Tachibana, 2012).…”

Section: Pendahuluanunclassified

“…Enzim Lac dan MnP termasuk enzim ekstraselular, sehingga penggunaan enzim ini dalam bidang bioteknologi sangat luas, mulai dari industri makanan, tektil, delignifikasi, produksi etanol, biosensor, dan bioremediasi Karigar & Rao, 2011;Larsson et al, 2001;Majeau, Brar, & Tyagi, 2010;Rodríguez Couto & Toca Herrera, 2006). Enzim Lac dan MnP masuk dalam kategori enzim oksidoreduksi, namun dalam aplikasi bioteknologi enzim Lac lebih mudah tersedia dan mudah dimanipulasi (Rodríguez Couto & Toca Herrera, 2006). Dalam proses delignifikasi (pembuatan bubur kertas dan bio-etanol), manipulasi tersebut penting dilakukan setelah pengembangan sistem biobleaching menunjukkan hasil yang kurang memuaskan.…”

Section: Seleksi Produksi Enzim Lac Dan Mnpunclassified

SELEKSI JAMUR PELAPUK PUTIH HUTAN TROPIS INDONESIA SEBAGAI PENGHASIL ENZIM LAKASE (Lac) DAN MANGAN PEROKSIDASE (MnP)

Efiyanti¹,

Hidayat²

2017

j.penelit.has.kehutan

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White-rot fungus, Basidiomycetes is an unique group of microbes among the major decomposers of plant polymers or biomass. Their existences are under pressure due to Indonesian tropical forests degradation caused by forest fires ABSTRAKJamur pelapuk putih Basidiomycetes adalah kelompok mikroba yang sangat unik. Secara alami mereka dapat mendekomposisi biomassa berlignoselulosa. Keberadaan hutan tropis Indonesia saat ini terus berkurang akibat kebakaran hutan, eksploitasi yang berlebihan, konversi lahan, dan biopiracy. Secara alami, jamur pelapuk putih berpotensi untuk dimanfaatkan sebagai bioresources, yaitu untuk meningkatkan citra rasa, kualitas, dan fungsi makanan (industri makanan), delignifikasi (pulp dan kertas), produksi etanol (biofuel), biosensor, dan bioremediasi. Tulisan ini mempelajari isolasi, seleksi, dan analisa potensi enzim ekstraseluler lakase (Lac) dan mangan peroksidase (MnP) dari jamur yang tumbuh di beberapa lokasi hutan tropis Indonesia. Sebanyak 178 sampel jamur pelapuk putih yang berasal dari hutan tropis di Indonesia (Jawa Barat, Jawa Timur, dan Kalimantan Timur) telah diisolasi dan diseleksi pada media RBBR. Hasil penelitian menunjukkan bahwa sebanyak 26 isolat murni yang berhasil diisolasi menunjukan laju perubahan warna RBBR yang berbeda, dan enam isolat diantaranya (JB-7.1.1,

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Inhibitors of Laccases: A Review

Cited by 32 publications

References 0 publications

Insect multicopper oxidases: Diversity, properties, and physiological roles

Insect multicopper oxidases: Diversity, properties, and physiological roles

Potential of acetylacetone as a mediator for Trametes versicolor laccase in enzymatic transformation of organic pollutants

SELEKSI JAMUR PELAPUK PUTIH HUTAN TROPIS INDONESIA SEBAGAI PENGHASIL ENZIM LAKASE (Lac) DAN MANGAN PEROKSIDASE (MnP)

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