Reversible immobilization of lipases on octyl-glutamic agarose beads: A mixed adsorption that reinforces enzyme immobilization

Rueda, Nazzoly; Santos, Cleiton S. Dos; Rodríguez, María Gabriela Lagos; Albuquerque, Tiago Lima de; Barbosa, Oveimar; Torres, Rodrigo; Ortíz, Claudia; Fernández-Lafuente, Roberto

doi:10.1016/j.molcatb.2016.03.002

Cited by 75 publications

(43 citation statements)

References 70 publications

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“…Another alternative is to maintain all enzyme-support interactions reversible, mixing interfacial activation (mainly hydrophobic) with other physical interactions of a fully different nature. Although this additional interaction could involve immobilized chelates (Zucca et al, 2016), thiol disulfide reactive groups (Brena et al, 1993;Grazú et al, 2003;Pavlovic et al, 2003), dyes (Yakup Arıca et al, 1998), etc., the only one that we have been able to find is the use of long acyl moieties mixed with anion or cation groups, using agarose beads (Rueda et al, 2016d(Rueda et al, , 2016a.…”

Section: Maintaining the Reversibility Of The Immobilizationmentioning

confidence: 99%

“…That way, immobilization may become a mixed one, making enzyme release very difficult. This has reduced lipase desorption in thermal or organic solvent inactivation, and permitted the reuse of the support after incubation with guanidine (Rueda et al, 2015a(Rueda et al, , 2016d(Rueda et al, , 2016a. Curiously, in certain cases great enzyme stabilization was observed when compared to the hydrophobic support (Rueda et al, 2015a(Rueda et al, , 2016d(Rueda et al, , 2016a.…”

Section: Maintaining the Reversibility Of The Immobilizationmentioning

confidence: 99%

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Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

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Lipases are the most widely used enzymes in biocatalysis, and the most utilized method for enzyme immobilization is using hydrophobic supports at low ionic strength. This method allows the one step immobilization, purification, stabilization, and hyperactivation of lipases, and that is the main cause of their popularity. This review focuses on these lipase immobilization supports. First, the advantages of these supports for lipase immobilization will be presented and the likeliest immobilization mechanism (interfacial activation on the support surface) will be revised. Then, its main shortcoming will be discussed: enzyme desorption under certain conditions (such as high temperature, presence of cosolvents or detergent molecules). Methods to overcome this problem include physical or chemical crosslinking of the immobilized enzyme molecules or using heterofunctional supports. Thus, supports containing hydrophobic acyl chain plus epoxy, glutaraldehyde, ionic, vinylsulfone or glyoxyl groups have been designed. This prevents enzyme desorption and improved enzyme stability, but it may have some limitations, that will be discussed and some additional solutions will be proposed (e.g., chemical amination of the enzyme to have a full covalent enzyme-support reaction). These immobilized lipases may be subject to unfolding and refolding strategies to reactivate inactivated enzymes. Finally, these biocatalysts have been used in new strategies for enzyme coimmobilization, where the most stable enzyme could be reutilized after desorption of the least stable one after its inactivation.

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Section: Maintaining the Reversibility Of The Immobilizationmentioning

confidence: 99%

Section: Maintaining the Reversibility Of The Immobilizationmentioning

confidence: 99%

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

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481

291

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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%

“…CALA has a large lid able to isolate the active center from the medium, 49,50 undergoes conventional interfacial activation upon adsorption on hydrophobic surfaces, 51 and has been immobilized in many hydrophobic supports. [52][53][54] CALB is a lipase having a very small lid that does not isolate the activity center from the medium. 51,55,56 That way, the hydrophobic pocket surrounding the active center is smaller than in the case of CALA, and the enzyme may be immobilized on hydrophobic surfaces, [57][58][59][60][61] but not in the open form of other lipases.…”

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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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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“…[27,28] Aw idely used strategy to overcome these problems is the immobilizationo ft he enzyme into as olid substrate. [29,30] Reported for the first time in 1916, [31] this methodhas grown significantly over the past decades allowing for the economicv iability of the use of several enzymes in industrial processes, causing ag reat economic and scientific impact.T he immobilization of enzymes on ah eterogeneous substrate promotes ac onvenient handling and af acile separation of the biocatalyst from the reaction medium. [32] Additionally,i to ften enhances enzyme stabilityt owards denaturation by autolysis, decomposition by organic solvents or by heat, as well as boosting the enzyme activity.…”

Section: Introductionmentioning

confidence: 99%

Enzyme‐Decorated Covalent Organic Frameworks as Nanoporous Platforms for Heterogeneous Biocatalysis

Oliveira

Souza

Bassut

et al. 2019

Chemistry A European J

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Sustainability in chemistry heavily relies on heterogeneous catalysis. Enzymes, the main catalyst for biochemical reactions in nature, are an elegant choice to catalyze reactions due to their high activity and selectivity, although they usually suffer from lack of robustness. To overcome this drawback, enzyme‐decorated nanoporous heterogeneous catalysts were developed. Three different approaches for Candida antarctica lipase B (CAL‐B) immobilization on a covalent organic framework (PPF‐2) were employed: physical adsorption on the surface, covalent attachment of the enzyme in functional groups on the surface and covalent attachment into a linker added post‐synthesis. The influence of the immobilization strategy on the enzyme uptake, specific activity, thermal stability, and the possibility of its use through multiple cycles was explored. High specific activities were observed for PPF‐2‐supported CAL‐B in the esterification of oleic acid with ethanol, ranging from 58 to 283 U mg−1, which was 2.6 to 12.7 times greater than the observed for the commercial Novozyme 435.

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Reversible immobilization of lipases on octyl-glutamic agarose beads: A mixed adsorption that reinforces enzyme immobilization

Cited by 75 publications

References 70 publications

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

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

Enzyme‐Decorated Covalent Organic Frameworks as Nanoporous Platforms for Heterogeneous Biocatalysis

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