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2017 | z. 81, nr 1 | 41--70
Tytuł artykułu

Laccases - Enzymes with an Unlimited Potential

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EN
Abstrakty
EN
Laccases (EC 1.10.3.2) are among the few enzymes, the history of which dates back to the 19th century. These oxidoreductases are present in almost all known fungi, some species of higher plants and insects. Moreover, in recent years, these enzymes have also been found in some bacterial organisms. Due to their significant properties and structure of the catalytic centre, laccases have been classified as the multicopper oxidases (MCOs). These enzymes are able to catalyse the oxidation of phenolic and non-phenolic compounds, with the aid of small molecules referred to as mediators. Thanks to their diverse nature, laccases have gained attention of both scientists and entrepreneurs from all over the world. Their significance is reflected in countless scientific and industrial applications, wherein laccases have become inseparable from chemical syntheses, the food industry, textile industry, biosensor design and the environmental protection. This paper gathers the most important information and the latest scientific discoveries relating to this desirable biocatalyst. (original abstract)
Słowa kluczowe
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Numer
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41--70
Opis fizyczny
Twórcy
  • Lodz University of Technology, Poland
  • Lodz University of Technology, Poland
  • Lodz University of Technology, Poland
  • Lodz University of Technology, Poland
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  • Nagai M, Kawata M, Watanabe H, Ogawa M, Saito K, Takesawa T, Kanda K, Sato T. Important role of fungal intracellular laccase for melanin synthesis: purification and characterization of an intracellular laccase from Lentinula edodes fruit bodies. Microbiol. Read. Engl 2003, 149:455-2462.
  • Golz-Berner K, Walzel B, Zastrow L, Doucet O. Cosmetic or dermatological preparation with skin-lightening Proteins. WO/2004/017931 2004, Retrieved July 24, 2015, from https://patentscope.wipo.int/search/en/detail.jsf?docId=WO2004017931.
  • Markussen EK, Jensen PE. Stabilisation of granules comprising active compounds. WO2006053564 A2 2006, Retrieved July 24, 2015, from http://www.google.ee/patents/WO2006053564A2.
  • Narise A, Takase T, Kikuchi S, Osawa K. Deodorizing composition under weak acidity. US20110033392 A1 2011, Retrieved July 24, 2015, from http://www.google.com.ar/patents/US20110033392.
  • Roggen EL, Ernst SE, Svendsen A, Friis EP, von der Osten C. Production and use of protein variants having modified immunogenecity 2015, Retrieved December 20, 2015, from http://www.google.com/patents/WO2001083559A2.
  • Haghighi B, Gorton L, Ruzgas T, Jönsson LJ. Characterization of graphite electrodes modified with laccase from Trametes versicolor and their use for bioelectrochemical monitoring of phenolic compounds in flow injection analysis. Anal Chim Acta 2003, 487:3-14.
  • Shleev S, Persson P, Shumakovich G, Mazhugo Y, Yaropolov A, Ruzgas T, Gorton L. Laccase-based biosensors for monitoring lignin. Enzyme Microb Technol 2006, 39:835-840.
  • Palanisamy S, Ramaraj SK, Chen S-M, Yang T, Yi-Fan P, Chen T-W, Velusamy V, Selvam S. A novel laccase biosensor based on laccase immobilized graphene cellulose microfiber composite modified screen-printed carbon electrode for sensitive determination of catechol. Sci Rep 2017, 7(41214):1-12.
  • Medina-Plaza C, de Saja JA, Rodriguez-Mendez ML. Bioelectronic tongue based on lipidic nanostructured layers containing phenol oxidases and lutetium bisphthalocyanine for the analysis of grapes. Biosens Bioelectron 2014, 57:276-283.
  • Mate DM, Gonzalez-Perez D, Falk M, Kittl R, Pita M, De Lacey AL, Ludwiq R, Shleev S, Alcalde M. Blood tolerant laccase by directed evolution. Chem Biol 2013, 20:223-231.
  • Barrière F, Kavanagh P, Leech D. A laccase-glucose oxidase biofuel cell prototype operating in a physiological buffer. Electrochimica Acta 2006, 51:5187-5192.
  • Almeira I, Henriques F, Calvalho M, Viana A. Carbon disulfide mediated selfassembly of laccase and iron oxide nanoparticles on gold surfaces for biosensing applications. J Colloid Interface Sci 2017, 485:242-250.
  • Sun J, Zheng M, Lu Z, Lu F, Zhang C. Heterologous production of a temperature and pH-stable laccase from Bacillus vallismortis fmb-103 in Escherichia coli and its application. Process Biochem 2017, in press, http://dx.doi.org/10.1016/j.procbio.2017.01.030.
Typ dokumentu
Bibliografia
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Identyfikator YADDA
bwmeta1.element.ekon-element-000171577930

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