Enzyme immobilization on epoxy supports in reverse micellar media: Prevention of enzyme denaturation

Thudi, Lahari; Jasti, Lakshmi Swarnalatha; Swarnalatha, Y.; Fadnavis, Nitin W.; Mulani, Khudbudin; Deokar, Sarika; Ponrathnam, S.

doi:10.1016/j.molcatb.2011.08.014

Cited by 22 publications

(6 citation statements)

References 54 publications

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“…An interesting approach to the immobilization of enzymes is also the use of reverse micelles (Thudi et al 2012), in which the hydrophobic part is directed outside the micelle to allow an enzyme attachment.…”

Section: Organic 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: Organic Carriersmentioning

confidence: 99%

“…Typical compounds meeting this condition are bifunctional carbonyl compounds, among them glutaraldehyde being apparently most common (see Fig. 4) (Delvaux and Demoustier-Champagne 2003;de Lathouder et al 2008;Thudi et al 2012). Glutaraldehyde with the formula CH 2 (CH 2 CHO) 2 contains two reactive aldehyde groups.…”

Section: Surface Modifying Agentsmentioning

confidence: 99%

Enzyme immobilization by adsorption: a review

2014

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“…But entrapment of GOx/HRP/o-dianisidine in reverse micelle is not exactly immobilization as we observed on solid support. The assemblies are dynamic species and inter-micellar exchange of molecules including proteins is quite fast [38,39] and it causes a rearrangement of reverse micellar aggregates and affect the equilibrium of the system [40]. These systems may show instability like phase separation, sedimentation or creaming due to coalescence and Ostwald's ripening which will affect their application in enzyme catalysis [41].…”

Section: Encapsulation Of Go X In Microemulsionmentioning

confidence: 99%

Entrapment of Glucose Oxidase in Reverse Micelle Microemulsion Systems for Glucose Detection in Lipid Based Food Products

et al. 2019

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Entrapment of glucose oxidase (GOx) enzyme in a new reverse micelle emulsion system was studied. The microemulsion consists of aqueous phase (buffered enzyme)/SPAN 85/n-decane. Critical micelle concentration (CMC) of surfactant-SPAN 85 in n-decane was determined using dynamic light scattering study and it was used to develop microemulsion system. Most stable and optically transparent microemulsion with entrapped glucose oxidase showed higher values of specific enzyme activity, maximum reaction rate (Vmax) and turn over number and low value of Michaelis-constant (Km) in comparison to homogeneous GOx (enzyme-glucose oxidase) system. The microemulsion system was successfully used to quantify D-glucose in lipid based food products without any sample preparation. Comparison of these results with chemical method (phenol-sulfuric acid method) and commercial kit method used in food industry validate the efficiency of the new proposed system. The study provides new information about the glucose content of some commonly consumed milk based products where nutritional labels do not accurately show true glucose content. These findings provide support for comprehensive glucose labeling to food products commonly used by the children.

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“…Immobilization on optimally designed synthetic supports can provide enzymes with remarkable properties, including dramatically enhanced stability against thermal − and chemical − deactivation, while also increasing enzyme activity and improving the ease of recycling. Owing to these advantages, enzyme immobilization has gained widespread interest in many fields, including chemical, and pharmaceutical production, − biosensing, − and bioremediation. − Additionally, a growing emphasis on sustainability is driving a shift toward enzyme-based industrial bioprocesses to reduce the use of supported metals and organocatalysts. − Recent breakthroughs have underscored the remarkable potential of complex heterogeneous and dynamic materials, including lipid bilayers , and copolymer brushes − , as robust supports for enzyme immobilization.…”

Section: Introductionmentioning

confidence: 99%

Combinatorial High-Throughput Screening of Complex Polymeric Enzyme Immobilization Supports

Sánchez-Morán,

Kaar,

Schwartz

2024

J. Am. Chem. Soc.

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Recent advances have demonstrated the promise of complex multicomponent polymeric supports to enable suprabiological enzyme performance. However, the discovery of such supports has been limited by time-consuming, low-throughput synthesis and screening. Here, we describe a novel combinatorial and high-throughput platform that enables rapid screening of complex and heterogeneous copolymer brushes as enzyme immobilization supports, named combinatorial high-throughput enzyme support screening (CHESS). Using a 384-well plate format, we synthesized arrays of three-component polymer brushes in the microwells using photoactivated surface-initiated polymerization and immobilized enzymes in situ. The utility of CHESS to identify optimal immobilization supports under thermally and chemically denaturing conditions was demonstrated usingBacillus subtilisLipase A (LipA). The identification of supports with optimal compositions was validated by immobilizing LipA on polymer-brush-modified biocatalyst particles. We further demonstrated that CHESS could be used to predict the optimal composition of polymer brushes a priori for the previously unexplored enzyme, alkaline phosphatase (AlkP). Our findings demonstrate that CHESS represents a predictable and reliable platform for dramatically accelerating the search of chemical compositions for immobilization supports and further facilitates the discovery of biocompatible and stabilizing materials.

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Enzyme immobilization on epoxy supports in reverse micellar media: Prevention of enzyme denaturation

Cited by 22 publications

References 54 publications

Enzyme immobilization by adsorption: a review

Enzyme immobilization by adsorption: a review

Entrapment of Glucose Oxidase in Reverse Micelle Microemulsion Systems for Glucose Detection in Lipid Based Food Products

Combinatorial High-Throughput Screening of Complex Polymeric Enzyme Immobilization Supports

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