Immobilization and stabilization of different β-glucosidases using the glutaraldehyde chemistry: Optimal protocol depends on the enzyme

Andrades, Diandra de; Graebin, Natália G.; Kadowaki, Marina Kimiko; Ayub, Marco Antônio Záchia; Fernández-Lafuente, Roberto; Rodrigues, Rafael C.

doi:10.1016/j.ijbiomac.2019.02.057

Cited by 88 publications

(40 citation statements)

References 49 publications

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“…These results corroborate the expected reaction property that, as pH increases, so does the reactivity of the enzyme versus the vinylsulfone groups on the support . However, the immobilization rate was not high as in other cases, very likely because this enzyme is also very glycosylated.…”

Section: Resultssupporting

confidence: 83%

“…These results corroborate the expected reaction property that, as pH increases, so does the reactivity of the enzyme versus the vinylsulfone groups on the support. 27 However, the immobilization rate was not high as in other cases, 42,47 very likely because this enzyme is also very glycosylated. β-Glucosidase from Celluclast ® 1.5L was also immobilized on glyoxyl-agarose reaching an immobilization yield of 49% (Figure 3e).…”

Section: β-Glucosidases Immobilizationmentioning

confidence: 81%

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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.

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Section: Resultssupporting

confidence: 83%

Section: β-Glucosidases Immobilizationmentioning

confidence: 81%

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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“…BG has been covalently immobilized on a variety of supports [17][18][19][20][21][22]. Covalent binding on chitosan led to enhanced BG thermal and storage stability [17], but chitosan has limited industrial applications for its very soft texture and density similar to water.…”

Section: Introductionmentioning

confidence: 99%

Covalent Immobilization of β-Glucosidase into Mesoporous Silica Nanoparticles from Anhydrous Acetone Enhances Its Catalytic Performance

et al. 2020

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An immobilization protocol of a model enzyme into silica nanoparticles was applied. This protocol exploited the use of the bifunctional molecule triethoxysilylpropylisocyanate (TEPI) for covalent binding through a linker of suitable length. The enzyme β-glucosidase (BG) was anchored onto wrinkled silica nanoparticles (WSNs). BG represents a bottleneck in the conversion of lignocellulosic biomass into biofuels through cellulose hydrolysis and fermentation. The key aspect of the procedure was the use of an organic solvent (anhydrous acetone) in which the enzyme was not soluble. This aimed to restrict its conformational changes and thus preserve its native structure. This approach led to a biocatalyst with improved thermal stability, characterized by high immobilization efficiency and yield. It was found that the apparent KM value was about half of that of the free enzyme. The Vmax was about the same than that of the free enzyme. The biocatalyst showed a high operational stability, losing only 30% of its activity after seven reuses.

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“…It should be considered anyway that in these papers, the versatility of glutaraldehyde was not applied to obtain the most active and stable biocatalyst [53,[105][106][107][108][109]. The same situation occurs with the genipin, since generally only one condition is used (Figure 7).…”

Section: Enzyme Immobilization On Preexisting Supports Using Genipinmentioning

confidence: 99%

Genipin as An Emergent Tool in the Design of Biocatalysts: Mechanism of Reaction and Applications

et al. 2019

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Genipin is a reagent isolated from the Gardenia jasminoides fruit extract, and whose low toxicity and good crosslinking properties have converted it into a reactive whose popularity is increasing by the day. These properties have made it widely used in many medical applications, mainly in the production of chitosan materials (crosslinked by this reactive), biological scaffolds for tissue engineering, and nanoparticles of chitosan and nanogels of proteins for controlled drug delivery, the genipin crosslinking being a key point to strengthen the stability of these materials. This review is focused on the mechanism of reaction of this reagent and its use in the design of biocatalysts, where genipin plays a double role, as a support activating agent and as inter- or intramolecular crosslinker. Its low toxicity makes this compound an ideal alterative to glutaraldehyde in these processes. Moreover, in some cases the features of the biocatalysts prepared using genipin surpassed those of the biocatalysts prepared using other standard crosslinkers, even disregarding toxicity. In this way, genipin is a very promising reagent in the design of biocatalysts.

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Immobilization and stabilization of different β-glucosidases using the glutaraldehyde chemistry: Optimal protocol depends on the enzyme

Cited by 88 publications

References 49 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

Covalent Immobilization of β-Glucosidase into Mesoporous Silica Nanoparticles from Anhydrous Acetone Enhances Its Catalytic Performance

Genipin as An Emergent Tool in the Design of Biocatalysts: Mechanism of Reaction and Applications

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