Immobilization of lipase from Candida rugosa on Eupergit® C supports by covalent attachment

Knežević, Zorica; Milosavić, Nenad; Bezbradica, Dejan; Jakovljević, Živana; Prodanović, Radivoje

doi:10.1016/j.bej.2006.05.009

Cited by 157 publications

(93 citation statements)

References 34 publications

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“…For example, the increase in laccase load from 22 to 440 mg/g resulted in the decrease of activity recovery: from 36.1 to 21.1% for Eupergit C and more so, from 88.4 to 43.8%, in the case of Eupergit C 250L. It is generally acknowledged that the immobilisation efficiency of enzymes on solid supports decreases when enzyme loading exceeds a certain value (Knezevic et al 2006;Li et al 2007). In fact, it was observed that Eupergit carriers presented a saturation value of laccase of 440 mg protein/g support.…”

Section: Immobilisation Of Laccasementioning

confidence: 99%

“…The application of covalent immobilisation techniques considers two different possibilities: either the use of inert carriers which can be properly activated or even the use of active supports commercially available. Among the latter, Eupergit carriers have been reported to be effective supports for immobilisation of laccase (Hublik and Schinner 2000;Katchalski-Katzir and Kraemer 2000;Knezevic et al 2006;Russo et al 2008). Eupergit supports (epoxy-activated acrylic polymers) have been developed between 1974 and 1980 by Röhm, Darmstadt, Germany.…”

Section: Introductionmentioning

confidence: 99%

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Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat lower catalytic efficiency (based on the ratio between the turnover number and the Michaelis constant, k cat /K M ) of the immobilised enzyme in comparison with that of the free enzyme was balanced by its increased stability and broader operational window related to temperature and pH. The feasibility of the immobilised laccase was tested by using a packed bed reactor (PBR) operating in consecutive cycles for the removal of Acid Green 27 dye as model substrate. High degrees of elimination were achieved (88, 79, 69 and 57% in 4 consecutive cycles), while the levels of adsorption on the support varied from 18 to 6%, proving that dye removal took place mainly due to the action of the enzyme. Finally, a continuous PBR with the solid biocatalyst was applied for the treatment of a solution containing the following endocrine disrupting chemicals: estrone (E1), 17b-estradiol (E2) and 17a-ethinylestradiol (EE2). At steady-state operation, E1 was degraded by 65% and E2 and EE2 were removed up to 80% and only limited adsorption of these compounds on the support, between 12 and 22%, was detected. In addition, a 79% decrease in estrogenic activity was detected in the effluent of the enzymatic reactor while only 14% was attained by inactivated laccase.

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Section: Immobilisation Of Laccasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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“…Based on those functional groups, Foresti et al pre-introduced 1,2-diaminoethane and glutaraldehyde as a spacer arm onto the surface of Eupergit Ⓡ C following the immobilization of CRL. Compared to the direct lipase binding to Eupergit Ⓡ C method, the latter increased the flexibility and activity of the immobilized enzymes (19). Similarly, in the study by Miletic et al, crosslinked macroporous hydrophilic poly (glycidyl methacrylate-co-ethylene glycol dimethacrylate) (poly(GMA-co-EGDMA)) were synthesized via suspension polymerization and then went through glutaraldehyde and cyanuric chloride modification process.…”

Section: Surface Attachment Immobilization Of Enzymes On Polymer Suppmentioning

confidence: 99%

“…In order to overcome this limitation, a flexible spacer is often introduced onto the supports. It has been mentioned that Eupergit Ⓡ C resins can be directly used for lipase immobilization via their oxirane groups (15)(16)(17)(18)(19). Based on those functional groups, Foresti et al pre-introduced 1,2-diaminoethane and glutaraldehyde as a spacer arm onto the surface of Eupergit Ⓡ C following the immobilization of CRL.…”

Section: Surface Attachment Immobilization Of Enzymes On Polymer Suppmentioning

confidence: 99%

Polymer materials for enzyme immobilization and their application in bioreactors

Fang¹,

Huang²,

Chen³

et al. 2011

BMB Reports

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Enzymatic catalysis has been pursued extensively in a wide range of important chemical processes for their unparalleled selectivity and mild reaction conditions. However, enzymes are usually costly and easy to inactivate in their free forms. Immobilization is the key to optimizing the in-service performance of an enzyme in industrial processes, particularly in the field of non-aqueous phase catalysis. Since the immobilization process for enzymes will inevitably result in some loss of activity, improving the activity retention of the immobilized enzyme is critical. To some extent, the performance of an immobilized enzyme is mainly governed by the supports used for immobilization, thus it is important to fully understand the properties of supporting materials and immobilization processes. In recent years, there has been growing concern in using polymeric materials as supports for their good mechanical and easily adjustable properties. Furthermore, a great many work has been done in order to improve the activity retention and stabilities of immobilized enzymes. Some introduce a spacer arm onto the support surface to improve the enzyme mobility. The support surface is also modified towards biocompatibility to reduce non-biospecific interactions between the enzyme and support. Besides, natural materials can be used directly as supporting materials owning to their inert and biocompatible properties. This review is focused on recent advances in using polymeric materials as hosts for lipase immobilization by two different methods, surface attachment and encapsulation. Polymeric materials of different forms, such as particles, membranes and nanofibers, are discussed in detail. The prospective applications of immobilized enzymes, especially the enzyme-immobilized membrane bioreactors (EMBR) are also discussed. [BMB reports 2011; 44(2): 87-95]

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“…According to the presence of certain groups, appropriate method of chemical activation is chosen. It is very important that the immobilization of lipase by covalent attachment to a support should involve only functional groups of the lipase that are not essential for its catalytic activity (Knežević et al 2006;Prlainović et al 2011). When it comes to supports with carboxy groups, enzymes are immobilized on the polymers through their amino groups, forming a peptide bond, with the presence of carbodiimide as a carboxy activator group.…”

Section: Shah and Gupta Immobilizedmentioning

confidence: 99%

Biodiesel Fuel Production by Enzymatic Transesterification of Oils: Recent Trends, Challenges and Future Perspectives

Luković¹,

Knežević‐Jugović²,

Bezbradica³

2011

Alternative Fuel

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Immobilization of lipase from Candida rugosa on Eupergit® C supports by covalent attachment

Cited by 157 publications

References 34 publications

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Polymer materials for enzyme immobilization and their application in bioreactors

Biodiesel Fuel Production by Enzymatic Transesterification of Oils: Recent Trends, Challenges and Future Perspectives

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