Immobilization of lipases on glyoxyl–octyl supports: Improved stability and reactivation strategies

Suescun, Angélica; Rueda, Nazzoly; Santos, José Cleiton Sousa dos; Castillo, Jaime; Ortíz, Claudia; Torres, Rodrigo; Barbosa, Oveimar; Fernández-Lafuente, Roberto

doi:10.1016/j.procbio.2015.05.010

Cited by 72 publications

(59 citation statements)

References 59 publications

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“…CALA has a large lid able to isolate the active center from the medium, undergoes conventional interfacial activation upon adsorption on hydrophobic surfaces, and has been immobilized in many hydrophobic supports . CALB is a lipase having a very small lid that does not isolate the activity center from the medium .…”

Section: Introductionmentioning

confidence: 99%

“…The further coating of these biocatalysts with polyethylenimine (PEI) has been reported to prevent one of the main problems of this immobilization protocol: the enzyme release under drastic conditions (high temperatures and organic cosolvents) or when used in reactions involving compounds with detergent features (fatty acids, partial glycerides, and even di or monoacetin) . The physical intermolecular crosslinking with PEI reduces this enzyme leakage, and it is a step in some coimmobilization strategies …”

Section: Introductionmentioning

confidence: 99%

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Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

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Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl‐agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p‐nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl‐CALA was less stable than octyl‐CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl‐CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl‐CALA permitted some stabilization. While octyl‐CALA was more active vs. pNPB, octyl‐CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 35: e2735, 2019

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

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“…OCGLX‐CALB maintained the initial rates and dibutyrin accumulation for 6 reaction cycles, while OC‐CALB activity dropped in the second reuse down to a negligible activity (Figure ). The higher stability of OCGLX compared to OC preparations, mainly inorganic media, had been previously stated and this case is a clear example . The likeliest explanation for this was the desorption of the enzyme from the support when using the OC preparation, due to the high concentration of the solvent and also to the high concentration of dibutyrin, that may be considered a mild detergent.…”

Section: Resultsmentioning

confidence: 51%

“…OCGLX was utilized to immobilize the enzymes in the cases where this support gave good results: CALB, Lecitase and CALA, while OCDVS was used for immobilizing RML, TLL and CRL . The covalent preparations were less active that the just adsorbed enzymes, even though using pNPB as substrate the activity was maintained after this covalent immobilization . RML and TLL immobilized on the heterofunctional supports decreased the yield of dibutyrin; apparently this was a better substrate and the yields of this compound significantly decreased (to fewer than 10 %).…”

Section: Resultsmentioning

confidence: 99%

“…However, it has a drawback: the desorption of the enzyme molecules under drastic conditions (e. g., high T or the presence of organic solvents or detergents) reduces their usefulness . This has been recently solved using heterofunctional supports that benefit from the interfacial activation of the lipase on a hydrophobic support which then permits their covalent attachment, using glyoxyl, glutaraldehyde, epoxide or divinylsulfone combined with acyl groups . In this respect, most lipases are 1,3 specific …”

Section: Introductionmentioning

confidence: 99%

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Advantages of Heterofunctional Octyl Supports: Production of 1,2-Dibutyrin by Specific and Selective Hydrolysis of Tributyrin Catalyzed by Immobilized Lipases

et al. 2016

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Different lipases immobilized on octyl agarose or heterofunctional (glyoxyl or divinylsulfone) octyl supports have been compared in the selective and specific production of 1,2‐dibutyrin by hydrolysis of tributyrin. The addition of cosolvents improved the solubility of the substrate thus improving the accumulation of 1,2‐dibutyrin. The form B of the lipase from Candida antarctica (CALB) was selected considering reaction both enzyme activity and reaction yields produced by this biocatalyst. Using this enzyme, the highest dibutyrin yield using 100 mM of tributyrin (over 80 %) was obtained using a medium containing 50 % of cosolvent. However, the use of higher tributyrin concentrations required increasing the concentration of cosolvent in order to increase the soluble fraction of substrate. Under these conditions, the enzyme is released to the medium if it is just physically adsorbed on the support. For this reason, the octyl‐CALB biocatalyst is unsuitable for this reaction. Using octyl‐glyoxyl‐CALB in the presence of 75 % cosolvent to facilitate substrate solubility, a conversion yield of 70 % of dibutyrin could be achieved using 1 M of tributyrin as substrate. Using 500 mM tributyrin, the yield under these conditions increased to 80 %. The biocatalyst could be reused for several cycles without any detrimental effect on its performance.

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An overview on the conversion of glycerol to value‐added industrial products via chemical and biochemical routes

Lima

Silva

Neto

et al. 2021

Biotech and App Biochem

106

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Glycerol is a common by-product of industrial biodiesel syntheses. Due to its properties, availability, and versatility, residual glycerol can be used as a raw material in the production of high value-added industrial inputs and outputs. In particular, products like hydrogen, propylene glycol, acrolein, epichlorohydrin, dioxalane and dioxane, glycerol carbonate, n-butanol, citric acid, ethanol, butanol, propionic acid, (mono-, di-, and triacylglycerols), cynamoil esters, glycerol acetate, benzoic acid, and other applications. In this context, the present study presents a critical evaluation of the innovative technologies based on the use of residual glycerol in different industries, including the pharmaceutical, textile, food, cosmetic, and energy sectors. Chemical and biochemical catalysts in the transformation of residual glycerol are explored, along with the factors to be considered regarding the choice of catalyst route used in the conversion process, aiming at improving the production of these industrial products.

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Immobilization of lipases on glyoxyl–octyl supports: Improved stability and reactivation strategies

Cited by 72 publications

References 59 publications

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Advantages of Heterofunctional Octyl Supports: Production of 1,2-Dibutyrin by Specific and Selective Hydrolysis of Tributyrin Catalyzed by Immobilized Lipases

An overview on the conversion of glycerol to value‐added industrial products via chemical and biochemical routes

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