Perspective of Recent Progress in Immobilization of Enzymes

Tran, Daniel; Balkus, Kenneth J.

doi:10.1021/cs200124a

Cited by 453 publications

(328 citation statements)

References 133 publications

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“…Prior work reporting enzyme encapsulation in porous silica materials with application to the cellulose to glucose to fructose conversion sequence, has been accomplished by two single enzyme nanospheres, where the two separate platforms were utilized sequentially [8,18]. Therefore, reaction conditions were not unified but changed for each sequential step to match the enzyme working conditions.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…In method (c), glutaraldehyde was used as a coupling agent [29,32] to promote the covalent grafting between the amino functions on the APTES-functionalized Si(HIPE) and the lysine residues of the enzyme (catalysts denoted "TA-Ax-GA" where GA stand for glutaraldehyde).…”

Section: Enzyme Immobilization On Si(hipe) Monolithsmentioning

confidence: 99%

“…For example, grafting amine groups on silica surface using (3-aminopropyl)triethoxysilane (APTES) favors electrostatic attraction between the silica carrier and the enzymes [27,28]. Furthermore, coupling agents such as glutaraldehyde can be used for the covalent cross-linking of enzymes through their lysine amino groups [29][30][31][32]. Thus, in this contribution, we make use of these structured Si(HIPE) supports and we implement several immobilization strategies to demonstrate the first example of a flow mode biocatalytic transamination process based on immobilized transaminases (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

Enantioselective Transamination in Continuous Flow Mode with Transaminase Immobilized in a Macrocellular Silica Monolith

Biggelaar¹,

Soumillion²,

Debecker³

2017

Preprint

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ω-Transaminases have been immobilized on macrocellular silica monoliths and used as heterogeneous biocatalysts in a continuous flow mode enantioselective transamination reaction. The support was prepared by a sol-gel method based on emulsion-templating. The enzyme was immobilized on the structured silica monoliths both by adsorption, and by covalent grafting using amino-functionalized silica monoliths and glutaraldehyde as a coupling agent. A simple reactor set-up based on the use of a heat-shrinkable Teflon tube is presented and successfully used for the continuous flow kinetic resolution of a chiral amine, 4-bromo-α-methylbenzylamine. The porous structure of the supports ensures effective mass transfer and the reactor works in the plug flow regime without preferential flow paths. When immobilized in the monolith and used in the flow reactor, transaminases retain their activity and their enantioselectivity. The solid biocatalyst is also shown to be stable both on stream and during storage. These essential features pave the way to the successful development of an environmentally friendly process for chiral amines production.

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“…[10][11][12][13][14][15] In spite of these attempts, a standard process for GOx immobilization has not yet been developed. Furthermore, GOx immobilization research to date has mostly focused on only increasing the amount of immobilized GOx without serious consideration of how to improve the electron transfer between the immobilized GOx molecules and supporter materials.…”

Section: Introductionmentioning

confidence: 99%

A new biocatalyst employing pyrenecarboxaldehyde as an anodic catalyst for enhancing the performance and stability of an enzymatic biofuel cell

2017

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A new enzyme catalyst consisting of pyrenecarboxaldehyde (PCA) and glucose oxidase (GOx) immobilized on polyethyleneimine (PEI) and a carbon nanotube supporter (CNT/PEI/[PCA/GOx]) is suggested, and the performance and stability of an enzymatic biofuel cell (EBC) using the new catalyst are evaluated. Using PCA, the amount of immobilized GOx increases (3.3 U mg − 1 ) and the electron transfer rate constant of the CNT/PEI/[PCA/GOx] is promoted (11.51 s − 1 ). Also, the catalyst induces excellent EBC performance (maximum power density (MPD) of 2.1 mW cm − 2 ), long-lasting stability (maintenance of 93% of the initial MPD after 4 weeks) and superior catalytic activity (flavin adenine dinucleotide redox reaction rate of 0.62 mA cm − 2 and Michaelis-Menten constant of 0.99 mM). These characteristics are ascribed to effects of (i) electron collection due to hydrophobic interactions, (ii) electron transfer pathways due to π-conjugated bonds and (iii) enzyme stabilization due to π-hydrogen bonds that are newly induced by the PCA/GOx composite. The existence of such positive interactions is properly verified using X-ray photoelectron spectroscopy and enzyme activity measurements. NPG Asia Materials (2017) 9, e386; doi:10.1038/am.2017.75; published online 2 June 2017 INTRODUCTIONThe demand for clean electrical energy is increasing as a result of weather changes caused by the greenhouse effect and depletion of fossil fuels. 1 To meet this demand, related research and development efforts are being eagerly pursued. As one of the efforts, enzymatic biofuel cells (EBCs) that convert bioenergy into electrical energy are being considered. 2,3 In particular, EBC systems employing glucose oxidase (GOx) as a biocatalyst have emerged because of their advantageous properties, such as biocompatibility, excellent selectivity toward specific substrates and strong activity near neutral pH and room temperature. 2 In addition, because EBC systems use human body-friendly fuels, such as glucose, glycerol, water and oxygen, for electricity generation, they can be embedded as power generators for the operation of artificial internal organs, such as artificial hearts and brains, insulin pumps or bone stimulators. [4][5][6][7][8] However, in spite of such promising facets of EBC systems, the commercialization of EBCs using GOx has been limited because of their low EBC performance and poor durability. 9 The disadvantages are attributed to the low immobilization ratio of GOx molecules, slow GOx-related reaction rate, low GOx activity and easy GOx denaturation. Of them, low GOx immobilization has been considered the main problem.

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Perspective of Recent Progress in Immobilization of Enzymes

Cited by 453 publications

References 133 publications

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

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

Enantioselective Transamination in Continuous Flow Mode with Transaminase Immobilized in a Macrocellular Silica Monolith

A new biocatalyst employing pyrenecarboxaldehyde as an anodic catalyst for enhancing the performance and stability of an enzymatic biofuel cell

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