Application of β-glucuronidase-immobilised silica gel formulation to microfluidic platform for biotransformation of β-glucuronides

Muderrisoglu, Cahit; Sargın, Sayıt; Yeşil-Çeliktaş, Özlem

doi:10.1007/s10529-018-2530-7

Cited by 8 publications

(7 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The efficiency is equal to 1 independently from the reaction temperature, suggesting that there is no internal mass transfer limitation. This KM decrease was also reported previously [34,35]. It is assumed that better mass transfer and heat transfer in the continuous case with respect to the batch case contribute to the improvement in kinetic parameters.…”

Section: Reaction Testssupporting

confidence: 88%

Immobilization of β-Glucosidase over Structured Cordierite Monoliths Washcoated with Wrinkled Silica Nanoparticles

et al. 2020

View full text Add to dashboard Cite

The enzymatic conversion of biomass-derived compounds represents a key step in the biorefinery flowsheet, allowing low-temperature high-efficiency reactions. β-Glucosidases are able to hydrolyze cellobiose into glucose. Wrinkled silica nanoparticles (WSNs) were demonstrated to be a good support for the immobilization of β-glucosidases, showing better performance than free enzymes in batch reaction; on the other hand, immobilized enzyme microreactors (IEMs) are receiving significant attention, because small quantities of reagents can be used, and favorable heat and mass transfer can be achieved with respect to conventional batch systems. In this work, we prepared, characterized, and tested structured enzymatic reactor compounds by a honeycomb monolith, a WSN washcoat, and β-glucosidases as the active phase. Powder and structured materials were characterized by transmission electron microscopy (TEM), scanning electron microscopy (SEM), N2 physisorption, thermogravimetric analysis (TGA), and Fourier-transform infrared spectroscopy (FT-IR). Structured catalysts were tested under both batch and continuous flow reaction conditions and compared to powder catalysts (batch reaction). The WSN washcoat was attached well onto the monolith walls, as suggested by the negligible weight loss after ultrasound treatment; the WSNs preserved their shape, porosity, and individual nature when deposited onto the monolith walls. The immobilized enzyme microreactors proved to be very efficient in hydrolysis of cellobiose to glucose, showing a complete conversion under continuous flow reaction at a batch-equivalent contact time equal to 120 min vs. 24 h obtained in the batch experiments. The apparent KM value showed a 20-fold decrease with respect to the batch process, due to the absence of external diffusive transport limitations.

show abstract

Section: Reaction Testssupporting

confidence: 88%

Immobilization of β-Glucosidase over Structured Cordierite Monoliths Washcoated with Wrinkled Silica Nanoparticles

et al. 2020

View full text Add to dashboard Cite

show abstract

“…115,116 Adding polyethylene oxide to a TEOS derived silica gel of β-glucuronidase from Helix pomatia enabled the microfluidic (the reaction was operated in small quantities of liquids within narrow channels) hydrolysis of p-nitrophenyl-β-D-glucuronide ( pNP-GluA). 117 Enzymes can be entrapped in alumina (Boehmite) gels by sol-gel processes. Liu et al claimed that hydrophilic alumina had advantages over silica, particularly, the retention of activity at high enzyme loading and the immobilization of low isoelectric point enzymes.…”

Section: Sol-gel Methodsmentioning

confidence: 99%

Enzyme entrapment, biocatalyst immobilization without covalent attachment

2021

View full text Add to dashboard Cite

show abstract

“…An interesting example of enzyme sol-gel encapsulation for the development of a bioreactor was reported by Muderrisouglu and colleagues [69]. β-glucuronidase was immobilized into TEOS-poly ethylene oxide (PEO) derived gels.…”

Section: Enzyme Encapsulation In Silica Gels For Protein Delivery Bimentioning

confidence: 99%

“…It was found that the system was more efficient than the batch at a flux rate of 1 µL/min, but not at higher flux rate. However, the microfluidic platform maintained continuous catalytic activity for seven days [69].…”

Section: Enzyme Encapsulation In Silica Gels For Protein Delivery Bimentioning

confidence: 99%

More than a Confinement: “Soft” and “Hard” Enzyme Entrapment Modulates Biological Catalyst Function

et al. 2019

View full text Add to dashboard Cite

Catalysis makes chemical and biochemical reactions kinetically accessible. From a technological point of view, organic, inorganic, and biochemical catalysis is relevant for several applications, from industrial synthesis to biomedical, material, and food sciences. A heterogeneous catalyst, i.e., a catalyst confined in a different phase with respect to the reagents’ phase, requires either its physical confinement in an immobilization matrix or its physical adsorption on a surface. In this review, we will focus on the immobilization of biological catalysts, i.e., enzymes, by comparing hard and soft immobilization matrices and their effect on the modulation of the catalysts’ function. Indeed, unlike smaller molecules, the catalytic activity of protein catalysts depends on their structure, conformation, local environment, and dynamics, properties that can be strongly affected by the immobilization matrices, which, therefore, not only provide physical confinement, but also modulate catalysis.

show abstract

Application of β-glucuronidase-immobilised silica gel formulation to microfluidic platform for biotransformation of β-glucuronides

Abstract: These results revealed that usage of the microreactors has considerable potential to efficiently obtain bioactive GluA-free aglycons from various plant-derived β-glucuronides for pharmaceutical applications.

Cited by 8 publications

References 22 publications

Immobilization of β-Glucosidase over Structured Cordierite Monoliths Washcoated with Wrinkled Silica Nanoparticles

Immobilization of β-Glucosidase over Structured Cordierite Monoliths Washcoated with Wrinkled Silica Nanoparticles

Enzyme entrapment, biocatalyst immobilization without covalent attachment

More than a Confinement: “Soft” and “Hard” Enzyme Entrapment Modulates Biological Catalyst Function

Contact Info

Product

Resources

About