Highly enhanced activity and stability via affinity induced immobilization β-glucosidase from Aspergillus niger onto amino-based silica for the biotransformation of ginsenoside Rb1

Wu, Xiuhong; Qu, Boquan; Liu, Yongkang; Ren, Xingxuan; Wang, Shaoyan; Quan, Yanling

doi:10.1016/j.chroma.2021.462388

Cited by 14 publications

(8 citation statements)

References 52 publications

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“…Intriguingly, crude glycosidase obtained from Leuconostoc mesenteroides DC102 transforms Rb1 into compound K with a yield of 99% after 3 days cultivation ( Quan et al, 2011 ). In addition, an enzyme immobilization method was developed for the effective biotransformation of Rb1to Rd, and the catalytic efficiency of the immobilized β-glucosidase from Aspergillus niger was 3.30-fold higher than that of the free enzyme ( Wu et al, 2021 ). Ginsenoside Rb2 can be transformed to Rd in the treatment of α-L-Arabinopyranosidase ( Kim et al, 2020 ).…”

Section: The Biotransformation Of Major Ginsenosides Into Minor Ginse...mentioning

confidence: 99%

A review for discovering bioactive minor saponins and biotransformative metabolites in Panax quinquefolius L.

Yang

Deng²,

Liu³

et al. 2022

Front. Pharmacol.

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Panax quinquefolius L. has attracted extensive attention worldwide because of its prominent pharmacological properties on type 2 diabetes, cancers, central nervous system, and cardiovascular diseases. Ginsenosides are active phytochemicals of P. quinquefolius, which can be classified as propanaxdiol (PPD)-type, propanaxtriol (PPT)-type, oleanane-type, and ocotillol-type oligo-glycosides depending on the skeleton of aglycone. Recently, advanced analytical and isolated methods including ultra-performance liquid chromatography tandem with mass detector, preparative high-performance liquid chromatography, and high speed counter-current chromatography have been used to isolate and identify minor components in P. quinquefolius, which accelerates the clarification of the material basis. However, the poor bioavailability and undetermined bio-metabolism of most saponins have greatly hindered both the development of medicines and the identification of their real active constituents. Thus, it is essential to consider the bio-metabolism of constituents before and after absorption. In this review, we described the structures of minor ginsenosides in P. quinquefolius, including naturally occurring protype compounds and their in vivo metabolites. The preclinical and clinical pharmacological studies of the ginsenosides in the past few years were also summarized. The review will promote the reacquaint of minor saponins on the growing appreciation of their biological role in P. quinquefolius.

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Section: The Biotransformation Of Major Ginsenosides Into Minor Ginse...mentioning

confidence: 99%

A review for discovering bioactive minor saponins and biotransformative metabolites in Panax quinquefolius L.

Yang

Deng²,

Liu³

et al. 2022

Front. Pharmacol.

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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: 99%

“…Immobilization methods are crosslinking, adsorption, encapsulation, ion exchange, affinity, and covalent bonding [14]. Immobilization by adsorption (anion exchange) to porous material supports has proven to be a promising strategy for obtaining active and stable biocatalysts [15,16].…”

Section: Introductionmentioning

confidence: 99%

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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“…Active immobilization by adsorption (anion exchange based ionic adsorption) or covalent binding (via aldehyde chemistry) to porous material supports have been shown as a promising strategy to obtain active and stable catalysts of different βglucosidases. In these previous works, the focus of the immobilization design was obtaining high specific activity (similar to the free enzyme) and enhancing the stability under resting conditions, which represents a promising point for implementation [17,18,[24][25][26][27][28][29][30][31][32].…”

Section: Introductionmentioning

confidence: 99%

Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

Alvarez-Gonzalez¹,

Santos²,

Ladero³

et al. 2022

Catalysts

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Cellulose saccharification to glucose is an operation of paramount importance in the bioenergy sector and the chemical and food industries, while glucose is a critical platform chemical in the integrated biorefinery. Among the cellulose degrading enzymes, β-glucosidases are responsible for cellobiose hydrolysis, the final step in cellulose saccharification, which is usually the critical bottleneck for the whole cellulose saccharification process. The design of very active and stable β-glucosidase-based biocatalysts is a key strategy to implement an efficient saccharification process. Enzyme immobilization and reaction engineering are two fundamental tools for its understanding and implementation. Here, we have designed an immobilized-stabilized solid-supported β−glucosidase based on the glyoxyl immobilization chemistry applied in porous solid particles. The biocatalyst was stable at operational temperature and highly active, which allowed us to implement 25 °C as working temperature with a catalyst productivity of 109 mmol/min/gsupport. Cellobiose degradation was implemented in discontinuous stirred tank reactors, following which a simplified kinetic model was applied to assess the process limitations due to substrate and product inhibition. Finally, the reactive process was driven in a continuous flow fixed-bed reactor, achieving reaction intensification under mild operation conditions, reaching full cellobiose conversion of 34 g/L in a reaction time span of 20 min.

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Highly enhanced activity and stability via affinity induced immobilization β-glucosidase from Aspergillus niger onto amino-based silica for the biotransformation of ginsenoside Rb1

Cited by 14 publications

References 52 publications

A review for discovering bioactive minor saponins and biotransformative metabolites in Panax quinquefolius L.

A review for discovering bioactive minor saponins and biotransformative metabolites in Panax quinquefolius L.

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

Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

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