Laccase immobilization on the tailored cellulose-based Granocel carriers

Rekuć, Adriana; Kruczkiewicz, Paulina; Jastrzembska, Bogna; Liesienė, Jolanta; Peczyńska‐Czoch, Wanda; Bryjak, Jolanta

doi:10.1016/j.ijbiomac.2007.09.014

Cited by 43 publications

(17 citation statements)

References 29 publications

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“…The immobilized enzyme preparation retained 7% of the initial laccase activity in solution [38]. Extracellular laccase produced by Cerrena unicolor was immobilized covalently on various cellulose-based supports, and the retained activity was obtained up to 20% compared to the free counterpart [39]. In this work, the immobilized laccase retained 82.6% of its initial activity, and the obtained result is quite comparable with the related literature.…”

Section: Properties Of the Immobilized Laccasesupporting

confidence: 85%

Preparation and characterization of epoxy-functionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes

Bayramoğlu

Yılmaz

Arıca

2009

Bioprocess Biosyst Eng

112

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Cross-linked magnetic chitosan beads were prepared by phase-inversion technique in the presence of epichlorohydrin under alkaline condition, and used for covalent immobilization of laccase. The activity of the immobilized laccase on the magnetic chitosan was about 260 U (g/dry beads) with an enzyme loading of about 16.33 +/- 0.39 mg [(g/dry beads) mg/g]. Kinetic parameters, V (max) and K (m) values were determined as 21.7 U/mg protein and 9.4 microM for free enzyme, and 15.6 U/mg protein and 19.7 microM for the immobilized laccase, respectively. The operational and thermal stabilities of the immobilized laccase were improved compared to free counterpart. The immobilized laccase was operated in a batch reactor for the decolorization of reactive dyes from aqueous solution. The laccase immobilized on magnetic chitosan beads was very effective for removal of textile dyes from aqueous solution which creates an important environmental problem in the discharged textile dying solutions.

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Section: Properties Of the Immobilized Laccasesupporting

confidence: 85%

Preparation and characterization of epoxy-functionalized magnetic chitosan beads: laccase immobilized for degradation of reactive dyes

Bayramoğlu

Yılmaz

Arıca

2009

Bioprocess Biosyst Eng

112

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“…The best preparation with high activity and storage stability was obtained after immobilization of invertase on Granocel modified with pentaethylenehexamine that gave a 19-atom spacer arm, with wider pore diameters, higher amine groups content and activated by glutaraldehyde. Similar results and preferences for Granocel-carriers superstructure and modification were observed after immobilization of glucoamylase and laccase (Rekuć et al 2007). From the other hand, immobilization of trypsin on Granocel carriers revealed preference to DVS activation of non-modified carrier (Bryjak et al 2008).…”

Section: Discussionsupporting

confidence: 74%

Man-tailored cellulose-based carriers for invertase immobilization

2008

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Cellulose-based carriers Granocel were specially prepared and optimised for covalent immobilization of enzymes. The effects of carrier characteristics such as pore size, chemistry of anchor groups and their density on invertase immobilization efficiency were evaluated. It was found that the preferential adsorption/binding of the enzyme to a carrier during coupling and its activity after immobilization depended on microenvironmental effects created by hydrophilic surface of the carrier, functional groups and their activators. The best preparations (activity approx. 300 U/mL, high storage stability) were obtained for NH 2 -Granocel activated with glutaraldehyde. It is probably due to Granocel modification with pentaethylenehexamine that gave a 19-atom spacer arm. The enzyme concentration in coupling mixture was optimised as well. The kinetic parameters of sucrose hydrolysis for native and immobilized invertase were evaluated. Compared to the native invertase, K m value of immobilized enzyme was only twice higher with about three times lower substrate inhibition. Reaction runs in a well mixed batch reactors with native and immobilized invertase showed slightly slower reaction rate in the case of the enzyme covalently bound to Granocel. Very good stability of cellulose-based carrier was proved experimentally by 20 successive reaction runs in a batch reactor.

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“…Up to date, there is still a great interest to develop novel technologies for improving immobilization capacity and activity recovery of the immobilized laccase (Vakurov et al, 2009;Rekuc et al, 2008).…”

Section: Introductionmentioning

confidence: 99%