Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor

Damnjanović, Jasmina; Žuža, Milena; Savanović, Jova K.; Bezbradica, Dejan; Mijin, Dušan Ž.; Bošković‐Vragolović, Nevenka; Knežević‐Jugović, Zorica

doi:10.1016/j.molcatb.2011.11.009

Cited by 43 publications

(32 citation statements)

References 37 publications

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“…(A)).On the other hand, considering that in higher ionic strength buffer electrostatic interactions are suppressed, it is not surprising that in all preparations immobilized in 1 mol L −1 buffer significantly lower protein loadings were observed, with maximum approximately 320 mg enzyme g −1 support. Comparing these results with those obtained for immobilization of lipase onto commercial supports with epoxy functional groups, GFNS has 5‐ to 10‐fold higher loading capacity, confirming that the high specific surface of nano‐materials offers great advantages in enzyme immobilization.…”

Section: Resultssupporting

confidence: 52%

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Epoxy-silanization - tool for improvement of silica nanoparticles as support for lipase immobilization with respect to esterification activity

Banjanac

Mihailović

Prlainović

et al. 2016

J. Chem. Technol. Biotechnol.

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BACKGROUND: In this study, in order to obtain the best support for the immobilization of lipase from Candida rugosa (CRL), the procedure for chemical modification of fumed silica nanoparticles (FNS) with (3-Glycidyloxypropyl)trimethoxysilane (GOPTMS) was optimized by varying the amount of GOPTMS used and the duration of support modification. To evaluate the prospects of chemical modification of FNS surface on the immobilization process, the activity and thermal stability of lipase immobilized on GFNS was compared with lipase immobilized on FNS and cyanuric chloride functionalized amino silica (CCAFNS). RESULTS:The epoxy functionalized silica nanoparticles (GFNS) with 400-500 mol of introduced epoxy groups per g of support were the most efficient, since immobilized preparations in 1 mol L −1 buffer had the highest activity of approximately 1495 IU g −1 and a loading capacity of 294 mg g −1 . Lipase immobilized on GFNS exhibited 1.5-fold higher hydrolytic activity and 2-fold higher esterification activity in the synthesis of aroma esters than lipase immobilized on CCAFNS, while its thermal stability was similar to CCAFNS preparations. CONCLUSION: These results indicated that the type of modification of the FNS surface has an influence on the specificity of the immobilized lipase, since lipase immobilized on GFNS showed improved properties for ester synthesis which is a promising area for immobilized lipase application.

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Section: Resultssupporting

confidence: 52%

“…The majority of groups were introduced by 4 h, and longer reaction time (up to 24 h) did not significantly increase the group density. It also needs to be emphasized that the concentration of epoxy group achieved is significantly higher in comparison with commercial epoxy‐activated carriers such as Eupergit® 34 and Sepabeds® …”

Section: Resultsmentioning

confidence: 99%

Epoxy-silanization - tool for improvement of silica nanoparticles as support for lipase immobilization with respect to esterification activity

Banjanac

Mihailović

Prlainović

et al. 2016

J. Chem. Technol. Biotechnol.

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“…Decrease in the yield of erucic acid can be explained by an insufficient reaction time when the substrates go through the packed bed reactor. Short residence time led to reduction of contact time between substrates and the enzyme, causing insufficient conversion of substrates in the initial reaction time [30,31]. In order to select an optimum condition clearly to produce erucic acid enrichment, correlation between the content of erucic acid and the yield of erucic acid is depicted in Fig.…”

Section: Residence Timementioning

confidence: 99%

Enrichment of erucic acid from crambe oil in a recirculated packed bed reactor via lipase-catalyzed ethanolysis

Zhao

Kim

et al. 2013

Journal of Molecular Catalysis B: Enzymatic

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“…Reaction media were placed in closed 4 mL vials equipped with a gas bubbler heated at 70 °C in silicon carbide plates. Conversions were determined by GC–MS, while enantiomeric excesses were determined by GC‐FID …”

Section: Methodsmentioning

confidence: 99%

Immobilization of lipase B from Candida antarctica on epoxy‐functionalized silica: characterization and improving biocatalytic parameters

Souza

Almeida

Leão

et al. 2017

J of Chemical Tech & Biotech

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BACKGROUND: In this work, lipase B from Candida antarctica (CaLB) was immobilized on Purolite ® ECR8205F, Purolite ® ECR8214F and Immobead ® IB150 P epoxy resins with no modification to their surfaces. Biocatalysts were evaluated for thermal stability and applied in reactions of hydrolysis, esterification and the synthesis of glyceryl carbonate by transesterification with dimethyl-carbonate both with glycerol and Macauba oil as well as dynamic kinetic resolution of -methylbenzylamine, all of them compared with commercial Novozyme 435 ® .

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Covalently immobilized lipase catalyzing high-yielding optimized geranyl butyrate synthesis in a batch and fluidized bed reactor

Cited by 43 publications

References 37 publications

Epoxy-silanization - tool for improvement of silica nanoparticles as support for lipase immobilization with respect to esterification activity

Epoxy-silanization - tool for improvement of silica nanoparticles as support for lipase immobilization with respect to esterification activity

Enrichment of erucic acid from crambe oil in a recirculated packed bed reactor via lipase-catalyzed ethanolysis

Immobilization of lipase B from Candida antarctica on epoxy‐functionalized silica: characterization and improving biocatalytic parameters

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