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Design and Characterization of Immobilized Laccase.

Autoři: Ježová Jana | Horynová Milada | Šuláková Romana | Bílková Zuzana

Rok: 2005

Druh publikace: ostatní - přednáška nebo poster

Název zdroje: 11th International Symposium on Separation Sciences 2005

Název nakladatele: Univerzita Pardubice

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Jazyk	Název	Abstrakt	Klíčová slova
cze	Design a charakteristika imobilizované lakázy	určeno pro seznam publikací	Lakáza; imobilizace; enzymový reaktor; kinetické parametry
eng	Design and Characterization of Immobilized Laccase.	Laccase (E.C. 1.10.3.2, p-diphenol: O2 oxidoreductase) is multi-copper enzyme catalyzing the oxidation of p-diphenols with the concomitant reduction of molecular oxygen to water. It is glycoprotein, usually monomeric, heterogenous in its biochemical properties and molecular structure [1]. The substrate range is broad and includes polyphenols, methoxy-substituted monophenols, aromatic amines, benzenethiols, polymethoxybenzenes and other easily oxidizable compounds. The initial reaction products are oxygen-centered aryloxyradicals or cation radicals which undergo non-enzyme coupling reactions [2]. Enzyme laccase has found commercial applications in oxidation of dyes, polymerization of lignin and lignosulphonates, preparation of musts and wines, waste water treatment to improve the whiteness in a conventional bleaching of cotton and recently biostoning [3]. Immobilized enzyme technology has grown rapidly during last decades, the enzyme reactors have utilized in many application areas of biotechnology where specific modification of target molecules and/or catalysis of chemical reactions is needed [4]. Enzyme immobilization provides many advantages over use of enzymes in soluble form: controlled product formation, enhanced enzyme activity, simplified and efficient processing and enzyme reusability. The storage properties and the pH stability of enzymes are often improved by immobilization [5]. In order to characterize immobilized laccase, the kinetic parameters of soluble and immobilized enzyme were compared. The activity of laccase was measured kinetically using two substrates: syringaldazine and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt. The Km values differed for individual substrates and also for soluble (0.012 mmol/l) and immobilized (0.0116 mmol/l) laccase. The magnetic form of macroporous bead cellulose (particle size of 80 ? 250 μm) served as the carrier. Two methods, oriented and non-oriented immobilization, were used t	laccase; immobilization; enzyme reactor; kinetic parameters

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