Easy stabilization of interfacially activated lipases using heterofunctional divinyl sulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironment

Albuquerque, Tiago Lima de; Rueda, Nazzoly; Santos, José Cleiton Sousa dos; Barbosa, Oveimar; Ortíz, Claudia; Bi̇nay, Barış; Özdemir, Ece; Gonçalves, Luciana Rocha Barros; Fernández‐Lafuente, Roberto

doi:10.1016/j.procbio.2016.04.002

Cited by 93 publications

(69 citation statements)

References 54 publications

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“…Blocking the support after immobilization is convenient to prevent any undesired enzyme‐support reaction. The change in the blocking reagent has been reported to affect enzyme activity and stability . In our case, the change of glycine for EDA did not change the enzyme activity.…”

Section: Resultscontrasting

confidence: 41%

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Preparation of immobilized/stabilized biocatalysts of β‐glucosidases from different sources: Importance of the support active groups and the immobilization protocol

Andrades

Graebin

Ayub

et al. 2019

Biotechnology Progress

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β‐Glucosidases from two different commercial preparations, Pectinex Ultra SP‐L and Celluclast® 1.5L, were immobilized on divinylsulfone (DVS) supports at pH 5.0, 7.0, 9.0, and 10. In addition, the biocatalysts were also immobilized in agarose beads activated by glyoxyl, and epoxide as reagent groups. The best immobilization results were observed using higher pH values on DVS‐agarose, and for Celluclast® 1.5L, good results were also obtained using the glyoxil‐agarose immobilization. The biocatalyst obtained using Pectinex Ultra SP‐L showed the highest thermal stability, at 65°C, and an operational stability of 67% of activity after 10 reuses cycles when immobilized on DVS‐agarose immobilized at pH 10 and blocked with ethylenediamine. The β‐glucosidase from Celluclast® 1.5L produced best results when immobilized on DVS‐agarose immobilized at pH 9 and blocked with glycine, reaching 7.76‐fold higher thermal stability compared to its free form and maintaining 76% of its activity after 10 successive cycles. The new biocatalysts obtained by these protocols showed reduction of glucose inhibition of enzymes, demonstrating the influence of immobilization protocols, pH, and blocking agent.

show abstract

Section: Resultscontrasting

confidence: 41%

“…The change in the blocking reagent has been reported to affect enzyme activity and stability. 28,[48][49][50] In our case, the change of glycine for EDA did not change the enzyme activity. Thus, the derivative blocked with glycine was also tested for glucose inhibition and thermal stability.…”

Section: β-Glucosidases Immobilizationcontrasting

confidence: 39%

Preparation of immobilized/stabilized biocatalysts of β‐glucosidases from different sources: Importance of the support active groups and the immobilization protocol

Andrades

Graebin

Ayub

et al. 2019

Biotechnology Progress

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“…This polypeptide can rearrange and consequently leads to conformational changes of lipases at the interface of water and organic phases. As a result of this rearrangement near the lipase active center, a significant increase of enzyme activity is observed [3][4][5][6]. Free form of lipase has a poor stability and it is not possible to use this enzyme in several catalytic cycles.…”

Section: Introductionmentioning

confidence: 99%

Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid

Ziegler-Borowska

Chełminiak-Dudkiewicz

Siódmiak

et al. 2017

Catalysts

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This article presents a novel route for crosslinking a polysaccharide and polysaccharide/protein shell coated on magnetic nanoparticles (MNPs) surface via condensation reaction with squaric acid (SqA). The syntheses of four new types of collagen-, chitosan-, and chitosan-collagen coated magnetic nanoparticles as supports for enzyme immobilization have been done. Structure and morphology of prepared new materials were characterized by attenuated total reflectance Fourier-transform infrared (ATR-FTIR), XRD, and TEM analysis. Next, the immobilization of lipase from Candida rugosa was performed on the nanoparticles surface via N-(3-dimethylaminopropyl)-N -ethylcarbodiimide hydrochloride (EDC)/N-hydroxy-succinimide (NHS) mechanism. The best results of lipase activity recovery and specific activities were observed for nanoparticles with polymer shell crosslinked via a novel procedure with squaric acid. The specific activity for lipase immobilized on materials crosslinked with SqA (52 U/mg lipase) was about 2-fold higher than for enzyme immobilized on MNPs with glutaraldehyde addition (26 U/mg lipase). Moreover, a little hyperactivation of lipase immobilized on nanoparticles with SqA was observed (104% and 112%).

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“…Today, a molecule can be immobilized into a molecular size cavity [2,128]. There have been reports on stability enhancement achieved by controlling the environment at a molecular level [129,130]. Through these immobilization techniques, enzyme-immobilized membranes that possess all the functions of the immobilized enzymes can be obtained, and it is believed that the membranes can be applied to various fields.…”

Section: Discussionmentioning

confidence: 99%

How to Lengthen the Long-Term Stability of Enzyme Membranes: Trends and Strategies

Yabuki

2017

Catalysts

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Abstract:In this review, factors that contribute to enhancing the stability of immobilized enzyme membranes have been indicated, and the solutions to each factor, based on examples, are discussed. The factors are divided into two categories: one is dependent on the improvement of enzyme properties, and the other, on the development of supporting materials. Improvement of an enzyme itself would effectively improve its properties. However, some novel materials or novel preparation methods are required for improving the properties of supporting materials. Examples have been provided principally aimed at improvements in membrane stability.

show abstract

Easy stabilization of interfacially activated lipases using heterofunctional divinyl sulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironment

Cited by 93 publications

References 54 publications

Preparation of immobilized/stabilized biocatalysts of β‐glucosidases from different sources: Importance of the support active groups and the immobilization protocol

Preparation of immobilized/stabilized biocatalysts of β‐glucosidases from different sources: Importance of the support active groups and the immobilization protocol

Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid

How to Lengthen the Long-Term Stability of Enzyme Membranes: Trends and Strategies

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