Co-immobilization of dextransucrase and dextranase in epoxy-agarose- tailoring oligosaccharides synthesis

Silva, Rhonyele Maciel da; Souza, Priscila Maria Paiva; Fernandes, Fabiano A. N.; Gonçalves, Luciana Rocha Barros

doi:10.1016/j.procbio.2019.01.009

Cited by 21 publications

(10 citation statements)

References 57 publications

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“…Glyoxyl support was prepared by etherification of agarose and glycidol and subsequent oxidation with periodate, according to protocol described by Guisán . The DVS‐agarose support was prepared activating the agarose matrix agarose with DVS as described by Ortega‐Muñoz et al To prepare the epoxy‐agarose support, the agarose beads were epoxylated with epichlorohydrin as previously reported …”

Section: Methodsmentioning

confidence: 99%

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.

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Section: Methodsmentioning

confidence: 99%

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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“…Many enzymes show maximum activity in aqueous media, and such enzymes can form compatible solutions for co-immobilization using aqueous polymer solutions. Certain natural polymers, like alginate, agarose and chitosan, are water-soluble, depending on pH, and can be mixed with enzymes to produce compatible solutions 155–157 that are then fabricated into different shapes, such as beads, 158 hydrogels, 159 capsules, 160 films, 161 particles, 162 nanoparticles, 163 and nanofibers. 164 Natural polymer derivatives ( e.g.…”

Section: Enzyme Immobilization Approachesmentioning

confidence: 99%

Enzyme immobilization: polymer–solvent–enzyme compatibility

Asaduzzaman

Salmon

2022

Mol. Syst. Des. Eng.

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“…The immobilization yield (Equation (1)), immobilization Other authors have reported outstanding reusability when using immobilized hydrolase systems, attributed to high retention of biocatalysts in the nanoparticles [11,17]. However, previous studies using a complex of hydrolytic enzymes immobilized on magnetic particles have reported activity drops to 20% after the second reuse cycle [16,28]. The reduction of the residual activity of the enzymes during the recycling test could be due to product inhibition, mechanical damage, or deactivation of the enzyme [31,32].…”

Section: Preparation Of Chitosan-coated Magnetite Particles (Fe3o4@chmentioning

confidence: 99%

“…Other shortcomings to consider are that when the least-stable enzyme is inactivated, both enzymes need to be discarded, and usually immobilization protocols on the same support may not be optimal for all enzymes [9,15]. Thus, efforts have been made to assess the impact of the immobilization procedure on operational stability, productivity, efficiency, and mass transfer within multienzymatic systems [16][17][18]. On the other hand, enzyme immobilization on a nano-polymeric matrix can improve enzyme stability as well as reuse capacity, but some drawbacks should be avoided, such as the cost of the fabrication process, large-scale application, and separation of the reaction medium [8].…”

Section: Introductionmentioning

confidence: 99%

Enhanced Performance of Immobilized Xylanase/Filter Paper-ase on a Magnetic Chitosan Support

et al. 2019

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Enzyme immobilization on different supports has emerged as an efficient and cost-effective tool to improve their stability and reuse capacity. This work aimed to produce a stable immobilized multienzymatic system of xylanase and filter paper-ase (FPase) onto magnetic chitosan using genipin as a cross-linking agent and to evaluate its biochemical properties and reuse capacity. A mixture of chitosan magnetic nanoparticles, xylanase, and FPase was covalently bonded using genipin. Immobilization yield and efficiency were quantified. The activity of free and immobilized enzymes was quantified at different values of pH, temperature, substrate concentration (Km and Vmax), and reuse cycles. The immobilization yield, immobilization efficiency, and activity recovery were 145.3% ± 3.06%, 14.8% ± 0.81%, and 21.5% ± 0.72%, respectively, measured as the total hydrolytic activity. Immobilization confers resistance to acidic/basic conditions and thermal stability compared to the free form. Immobilization improved 3.5-fold and 78-fold the catalytic efficiency (Kcat/Km) of the xylanase and filter paper-ase activities, while immobilized xylanase and FPase could be reused for 34 min and 43 min, respectively. Cross-linking significantly improved the biochemical properties of immobilized enzymes, combined with their simplicity of reuse due to the paramagnetic property of the support. Multienzyme immobilization technology is an important issue for industrial applications.

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Co-immobilization of dextransucrase and dextranase in epoxy-agarose- tailoring oligosaccharides synthesis

Cited by 21 publications

References 57 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

Enzyme immobilization: polymer–solvent–enzyme compatibility

Enhanced Performance of Immobilized Xylanase/Filter Paper-ase on a Magnetic Chitosan Support

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