Immobilization of β-glucosidase by self-catalysis and compared to crosslinking with glutaraldehyde

Naseer, Sidra; Ouyang, Jin; Chen, Xing; Pu, Shujin; Guo, Yanting; Zhang, Xuan; Li, Dali; Yang, Chengli

doi:10.1016/j.ijbiomac.2019.11.030

Cited by 39 publications

(12 citation statements)

References 21 publications

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“…Moreover, the immobilized β-glucosidase demonstrated a broader pH profile, which could be attributed to the protection given by the modified polyester support, as well as product buildup, which will, of course, impact the pH level in the vicinity of the immobilized β-glucosidase [ 35 ]. Similar pH profiles were observed in previous studies by Naseer et al [ 36 ] where β-glucosidase was cross-linked immobilized on SiO 2 nanoparticles. Gupta et al [ 37 ] reported that the alginate was employed as solid support for the encapsulation of β-glucosidase, and Çelik et al [ 38 ] reported that the enzyme was effectively immobilized on chitosan-multiwalled carbon nanotubes.…”

Section: Resultssupporting

confidence: 89%

“…The hydrolytic breakdown of the β-glycosidic bond between glucose and aryl or alkyl aglycone residues is catalyzed by this enzyme, which belongs to the hydrolase family [ 16 ].

-Glucosidase was immobilized using a variety of methods; for instance, it was immobilized on magnetic nanoparticles [ 17 ], on MnO 2 magnetic nanomaterial [ 18 ], and in SiO 2 nanoparticles using glutaraldehyde as a crosslink [ 19 ]. To the best of our knowledge, the immobilization of β-glucosidase on polyester treated with hydrazine hydrate and graphene oxide has not been reported to date.…”

Section: Introductionmentioning

confidence: 99%

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Polyester fabric modification by chemical treatment to enhancing the β-glucosidase immobilization

Almulaiky

2022

Heliyon

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Section: Resultssupporting

confidence: 89%

“…The hydrolytic breakdown of the β-glycosidic bond between glucose and aryl or alkyl aglycone residues is catalyzed by this enzyme, which belongs to the hydrolase family [ 16 ].

Section: Introductionmentioning

confidence: 99%

Polyester fabric modification by chemical treatment to enhancing the β-glucosidase immobilization

Almulaiky

2022

Heliyon

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“…Specific surface characteristics, surface area, and SiO 2 content also influenced the adsorption affinity and enzyme activity after immobilization [19]. Techniques for the immobilization of β-glucosidase through interactions such as covalent bonds and encapsulation have been previously reported; for example, it has been immobilized on magnetic nanoparticles with a binding efficiency of 96.5% [28], on amino-based silica with an immobilization efficiency 5.86 times that of the free enzyme [14], on a new magnetic nanomaterial of MnO 2 exhibiting greater thermal stability than the free one [29], in SiO 2 nanoparticles crosslinked with glutaraldehyde with an immobilization yield of 83.34% [30], on CNBr-activated Sepharose [31]. However, in this study, it is important to highlight that the increase in enzymatic activity during the immobilization process is related to the improvement of the adsorption affinity in the zeolite; furthermore, compared to covalent bonding, physical adsorption helps to maintain the structural conformation of the enzyme [32].…”

Section: Immobilization Processmentioning

confidence: 97%

Improvement in the Thermostability of a Recombinant β-Glucosidase Immobilized in Zeolite under Different Conditions

et al. 2022

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β-Glucosidase is part of the cellulases and is responsible for degrading cellobiose into glucose, a compound that can be used to produce biofuels. However, the use of the free enzyme makes the process more expensive. Enzyme immobilization improves catalytic characteristics and supports, such as zeolites, which have physical-chemical characteristics and ion exchange capacity that have a promising application in the biotechnological industry. This research aimed to immobilize by adsorption a recombinant β-glucosidase from Trichoderma reesei, obtained in Escherichia coli BL21 (DE3), in a commercial zeolite. A Box Behnken statistical design was applied to find the optimal immobilization parameters, the stability against pH and temperature was determined, and the immobilized enzyme was characterized by SEM. The highest enzymatic activity was determined with 100 mg of zeolite at 35 °C and 175 min. Compared to the free enzyme, the immobilized recombinant β-glucosidase presented greater activity from pH 2 to 4 and greater thermostability. The kinetic parameters were calculated, and a lower KM value was obtained for the immobilized enzyme compared to the free enzyme. The obtained immobilization parameters by a simple adsorption method and the significant operational stability indicate promising applications in different fields.

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“…Enzymes can catalyze many complex metabolisms in the human body through chemical reactions, and GOx is mostly used in glucose sensors ( Naghdi et al, 2018 ; Semwal and Gupta, 2018 ; Kahoush et al, 2019 ; Naseer et al, 2020 ). Glucose oxidase (β-D-glucose: oxygen-1-oxidoreductase) (GOD or GOx) is a homodimeric enzyme that is composed of two identical subunits and two non-covalently bound flavin adenine dinucleotides (FADs) ( Pazur and Kleppe, 1964 ; Kriechbaum et al, 1989 ).…”

Section: Electrospun Nanofiber-based Enzymatic and Non-enzymatic Gluc...mentioning

confidence: 99%

Electrospun nanofiber-based glucose sensors for glucose detection

Zhang

Liu

et al. 2022

Front. Chem.

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Diabetes is a chronic, systemic metabolic disease that leads to multiple complications, even death. Meanwhile, the number of people with diabetes worldwide is increasing year by year. Sensors play an important role in the development of biomedical devices. The development of efficient, stable, and inexpensive glucose sensors for the continuous monitoring of blood glucose levels has received widespread attention because they can provide reliable data for diabetes prevention and diagnosis. Electrospun nanofibers are new kinds of functional nanocomposites that show incredible capabilities for high-level biosensing. This article reviews glucose sensors based on electrospun nanofibers. The principles of the glucose sensor, the types of glucose measurement, and the glucose detection methods are briefly discussed. The principle of electrospinning and its applications and advantages in glucose sensors are then introduced. This article provides a comprehensive summary of the applications and advantages of polymers and nanomaterials in electrospun nanofiber-based glucose sensors. The relevant applications and comparisons of enzymatic and non-enzymatic nanofiber-based glucose sensors are discussed in detail. The main advantages and disadvantages of glucose sensors based on electrospun nanofibers are evaluated, and some solutions are proposed. Finally, potential commercial development and improved methods for glucose sensors based on electrospinning nanofibers are discussed.

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Immobilization of β-glucosidase by self-catalysis and compared to crosslinking with glutaraldehyde

Cited by 39 publications

References 21 publications

Polyester fabric modification by chemical treatment to enhancing the β-glucosidase immobilization

Polyester fabric modification by chemical treatment to enhancing the β-glucosidase immobilization

Improvement in the Thermostability of a Recombinant β-Glucosidase Immobilized in Zeolite under Different Conditions

Electrospun nanofiber-based glucose sensors for glucose detection

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