Synthesis of mesoporous silica with different pore sizes for cellulase immobilization: pure physical adsorption

Chen, Baiyi; Qiu, Jianhui; Mo, Haodao; Yu, Yanling; Ito, Kazushi; Sakai, Eiichi; Li, Congcong

doi:10.1039/c7nj00441a

Cited by 46 publications

(27 citation statements)

References 41 publications

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“…The adsorbed amount increased from 25 to 50 °C according to an Arrhenius-like trend. This indicates that the adsorption of cellulase on WSNs in endothermic in nature [ 12 , 34 ]. Adsorption at higher temperatures has not been analysed because enzymes are normally prone to thermal deactivation by denaturation.…”

Section: Resultsmentioning

confidence: 99%

“…For example, Zhang et al [ 35 ] covalently immobilized cellulase on silica gel substrate, retaining only 7% of its specific activity in the hydrolysis of CMC. Chen et al [ 12 ] immobilized cellulase on mesoporous silica with different pore size, obtaining at the best a retention of 63.3% of free cellulase activity. Takimoto et al [ 11 ] immobilized cellulase in SBA-15 with different pore size: the best biocatalyst preserved 67.5% of the activity of the free form.…”

Section: Resultsmentioning

confidence: 99%

“…In fact, when the pore size was just enough to host the cellulase, the enzyme remained close to the pore entrance, allowing an easy accessibly of its active site. Chen et al [ 12 ] synthesized two mesoporous silica with different pore size of 17.6 nm (MS-17.6) and 3.8 nm (MS-3.8). They used these mesoporous materials to immobilize cellulase from Acremonium by pure physical adsorption.…”

Section: Introductionmentioning

confidence: 99%

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Adsorption of Cellulase on Wrinkled Silica Nanoparticles with Enhanced Inter-Wrinkle Distance

et al. 2020

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Mesoporous silica materials offer a unique opportunity for enzyme immobilization thanks to their properties, such as tuneable pore size, large surface area and easy functionalization. However, a significant enhancement of cellulase enzyme activity entrapped inside the silica pores still represents a challenge. In this work, we immobilized cellulase by adsorption on wrinkled silica nanoparticles (WSNs), obtaining an active and stable biocatalyst. We used pentanol as co-solvent to synthesize WSNs with enhanced inter-wrinkle distance in order to improve cellulase hosting. The physical-chemical and morphological characterization of WSNs and cellulase/WSNs was performed by thermogravimetric (TG), Fourier transform infrared (FT-IR), and transmission electron microscopy (TEM) analyses. The obtained results showed that this matrix generates a favourable microenvironment for hosting cellulase. The results of the catalytic assays and operational stability confirmed the key role of size, morphology and distribution of the pores in the successful outcome of the cellulase immobilization process. The immobilization procedure used allowed preserving most of the secondary structure of the enzyme and, consequently, its catalytic activity. Moreover, the same value of glucose yield was observed for five consecutive runs, showing a high operational stability of the biocatalyst.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Adsorption of Cellulase on Wrinkled Silica Nanoparticles with Enhanced Inter-Wrinkle Distance

et al. 2020

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“…The increase in the apparent K M upon immobilization suggested mass transfer limitations, due to both the sticking of the nanoparticles and a crowding effect due to the excessive amount of enzyme inside the pores. The decrease in V max may be ascribed to detrimental modifications in the enzyme conformation for the bridging enzymes [50] and a loss of the conformational flexibility caused by interactions between the polypeptide molecules and with the matrix [58]. Concerning the immobilization of BG on nanoparticle carriers, Verma et al [27] immobilized a thermostable enzyme (β-glucosidase from Aspergillus niger) on functionalized magnetic nanoparticles by covalent binding.…”

Section: Resultsmentioning

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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“…Later, Chen et al found the similar result by using a mesoporous silica materials as the support for immobilizing cellulase. [ 24 ] The mesoporous silica with a pore size of 3.8 nm exhibited the best activity, which just matched the short axes of cellulase molecules. Washmon‐Kriel et al fabricated a novel hierarchical magnetic mesoporous silica microspheres with different pore sizes and open pore structures through a water/oil biphase synthetic strategy.…”

Section: Enzymatic Biosensorsmentioning

confidence: 98%

Mesoporous Materials–Based Electrochemical Biosensors from Enzymatic to Nonenzymatic

Yang

Qiu

Yang

et al. 2019

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Mesoporous materials have drawn more and more attention in the field of biosensors due to their high surface areas, large pore volumes, tunable pore sizes, as well as abundant frameworks. In this review, the progress on mesoporous materials–based biosensors from enzymatic to nonenzymatic are highlighted. First, recent advances on the application of mesoporous materials as supports to stabilize enzymes in enzymatic biosensing technology are summarized. Special emphasis is placed on the effect of pore size, pore structure, and surface functional groups of the support on the immobilization efficiency of enzymes and the biosensing performance. Then, the development of a nonenzymatic strategy that uses the intrinsic property of mesoporous materials (carbon, silica, metals, and composites) to mimic the behavior of enzymes for electrochemical sensing of some biomolecules is discussed. Finally, the challenges and perspective on the future development of biosensors based on mesoporous materials are proposed.

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Synthesis of mesoporous silica with different pore sizes for cellulase immobilization: pure physical adsorption

Abstract: The microstructure of mesoporous silica and their adsorbing cellulase process have been analyzed to investigating the physical adsorption mechanism.

Cited by 46 publications

References 41 publications

Adsorption of Cellulase on Wrinkled Silica Nanoparticles with Enhanced Inter-Wrinkle Distance

Adsorption of Cellulase on Wrinkled Silica Nanoparticles with Enhanced Inter-Wrinkle Distance

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

Mesoporous Materials–Based Electrochemical Biosensors from Enzymatic to Nonenzymatic

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