Immobilization of enzymes on porous silicas – benefits and challenges

Hartmann, Martin; Kostrov, Xenia

doi:10.1039/c3cs60021a

Cited by 558 publications

(382 citation statements)

References 58 publications

(157 reference statements)

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“…It is characterized by small pores, from 5 to about 30 nm in diameter and a hexagonal array of pores (Grudzień et al, 2006;2007;Hartmann and Kostrov 2013). Large volume of mesopores, close to 1.0 cm 3 /g and micropores of about 0.8 cm 3 /g, and also a very well developed surface area from 500 to 1400 m 2 /g [Hartmann and Kostrov 2013] make this silica an excellent support for the enzyme immobilization. Another mesoporous silica MSU-H (Yu and Fang 2013) has the specific surface area reaching 750 m 2 /g, pore radius from 7 to 10 nm and pore volume from 0.9 to 1.0 cm 3 /g.…”

Section: Inorganic Carriersmentioning

confidence: 99%

“…Among many inorganic carriers used for immobilization of enzymes by adsorption, silicas are apparently those carriers, which have drawn most attention (Erhardt and Jordening 2007;Magner 2013;Hartmann and Kostrov 2013). Silicas of different dispersive-morphological parameters and porous structures have been proposed.…”

Section: Inorganic Carriersmentioning

confidence: 99%

“…A representative silica used for the enzyme immobilization on a large scale is mesoporous silica SBA-15 (Santa Barbara Amorphous) with hexagonal array of pores (Salis et al 2010;Thorn et al 2011). It is characterized by small pores, from 5 to about 30 nm in diameter and a hexagonal array of pores (Grudzień et al, 2006;2007;Hartmann and Kostrov 2013). Large volume of mesopores, close to 1.0 cm 3 /g and micropores of about 0.8 cm 3 /g, and also a very well developed surface area from 500 to 1400 m 2 /g [Hartmann and Kostrov 2013] make this silica an excellent support for the enzyme immobilization.…”

Section: Inorganic Carriersmentioning

confidence: 99%

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Enzyme immobilization by adsorption: a review

2014

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Endowed with unparalleled high catalytic activity and selectivity, enzymes offer enormous potential as catalysts in practical applications. These applications, however, are seriously hampered by enzymes' low thermal and chemical stabilities. One way to improve these stabilities is the enzyme immobilization. Among various tested methods of this process that make use of different enzyme-carrier interactions, immobilization by adsorption on solid carriers has appeared most common. According to these findings, in this review we present a comparative analysis of the literature reports on the recent trends in the immobilization of the enzymes by adsorption. This thorough study was prepared in order to provide a deeper understanding of the process. Both carriers, carrier modifiers and procedures developed for effective adsorption of the enzymes are discussed. The review may thus be helpful in choosing the right adsorption scheme for a given enzyme to achieve the improvement of its stability and activity for a specific application.

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Section: Inorganic Carriersmentioning

confidence: 99%

Section: Inorganic Carriersmentioning

confidence: 99%

Section: Inorganic Carriersmentioning

confidence: 99%

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Enzyme immobilization by adsorption: a review

2014

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“…The supports can be either synthetic materials (mainly silicas) [11,12] or natural ones such as chitin and chitosan [13][14][15]. They are also characterized by high stability, well-developed surface area, and the possibility of surface functionalization with many modifying compounds [16,17].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Zdarta

Sałek

Kołodziejczak-Radzimska

et al. 2014

Open Chemistry

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The immobilization of Amano Lipase A fromAspergillus niger by adsorption onto Stöber silica matrix obtained by sol-gel method was studied. The effectiveness of the enzyme immobilization and thus the usefulness of the method was demonstrated by a number of physicochemical analysis techniques including Fourier Transform Infrared Spectroscopy (FT-IR), elemental analysis (EA), thermogravimetric analysis (TG), porous structure of the support and the products after immobilization from the enzyme solution with various concentration at different times. The analysis of the process' kinetics allowed the determination of the sorption parameters of the support and optimization of the process. The optimum initial concentration of the enzyme solution was found to be 5 mg mL -1 , while the optimum time of the immobilization was 120 minutes. These values of the variable parameters of the process were obtained by as ensuring the immobilization of the largest possible amount of the biocatalyst at the most economically beneficial aspects of the process.

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“…Several examples of enzyme immobilization onto porous silica have been reported [6][7][8][9][10][11][12]. Co-immobilization of enzymes on various platforms is an emerging field, and involves considerations of various factors: spanning from facile access of substrate to the next enzyme in the cascade, optimization of catalytic activity to allow performance of all components, and the stability of enzyme in the solid support [13].…”

Section: Introductionmentioning

confidence: 99%

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

Hsin¹,

Radu²,

Dezayas³

et al. 2017

J Thermodyn Catal

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The successful demonstration of a tandem enzymatic catalyst which utilizes stellate macroporous silica nanospheres (Stellate MSN) platform as dual-enzyme host is reported herein. Upon simultaneous loading of beta-glucosidase and glucose isomerase inside their porous structure, Stellate MSNs-featuring a hierarchical pore arrangement and large surface area, show capability to perform a cascade reaction that converts cellobiose, a cellulosic hydrolysis product, into glucose and further to fructose. The silica platform provides a modality for substrate channelling which involves the transfer of the cascade intermediate, glucose, to the next enzyme without first diffusing to the bulk. A key aspect to this proof-of-concept is the two-enzyme system working in an optimized pH domain to fit the modus operandi for both enzymes. The concept could be extrapolated to other enzyme tandems, with potential to impact dramatically enzymatic processes which require multi-catalyst, one-pot transformations.

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Immobilization of enzymes on porous silicas – benefits and challenges

Cited by 558 publications

References 58 publications

Enzyme immobilization by adsorption: a review

Enzyme immobilization by adsorption: a review

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

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