Methodological Approach for Modeling of Multienzyme in-pot Processes

Santacoloma, Paloma de Gracia Andrade; Martinez, Alicia Roman; Sin, Gürkan; Gernaey, Krist V.; Woodley, John M.

doi:10.1016/b978-0-444-54298-4.50048-9

Cited by 3 publications

(4 citation statements)

References 6 publications

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“…These hybrid architectures can deal with the intervening biological attributes by the virtue of reversible noncovalent electrostatic interactions, that is, hydrogen bonding, van der Waals forces, dispersion forces, π − π stacking interactions, dipole-dipole or ion-dipole interactions, halogen bonds, hydrophobic as well as coordination linkages, and irreversible chemistry of covalent interactions (Lehn, 1985). Intriguing features, namely homogeneity, reversibility, stimuli responsiveness, molecular recognition, selforganization, and exquisitely tunable characteristics of these supramolecules and multimolecular frameworks made them exclusively intellectual and insightful materials for the effective immobilization of biological entities (Pollard & Woodley, 2007;Santacoloma et al, 2011). Embedment of unique features in the designed supramolecular and multimolecular architectures with regulating size, shape, valency, and strength, intermolecular interactions enable them to construct the structures that seem to be appropriate for addressing the relevant biological issues (Uhlenheuer et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

A comprehensive review on bio‐mimicked multimolecular frameworks and supramolecules as scaffolds for enzyme immobilization

Aggarwal

Ikram

2022

Biotech & Bioengineering

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Immobilization depicts a propitious route to optimize the catalytic performances, efficient recovery, minimizing autocatalysis, and also augment the stabilities of enzymes, particularly in unnatural environments. In this opinion, supramolecules and multimolecular frameworks have captivated immense attention to achieve profound controllable interactions between enzyme molecules and well-defined natural or synthetic architectures to yield protein bioconjugates with high accessibility for substrate binding and enhanced enantioselectivities. This scholastic review emphasizes the possibilities of associating multimolecular complexes with biological entities via several types of interactions, namely covalent interactions, host-guest complexation, π − π interactions, intra/inter hydrogen bondings, electrostatic interactions, and so forth offers remarkable applications for the modulations of enzymes. The potential synergies between artificial supramolecular structures and biological systems are the primary concern of this pedagogical review. The majority of the research primarily focused on the dynamic biomolecule-responsive supramolecular assemblages and multimolecular architectures as ideal platforms for the recognition and modulation of proteins and cells. Embracing sustainable green demeanors of enzyme immobilizations in a quest to reinforce site-selectivity, catalytic efficiency, and structural integrality of enzymes are the contemporary requirements of the biotechnological sectors that instigate the development of novel biocatalytic systems.

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Section: Introductionmentioning

confidence: 99%

A comprehensive review on bio‐mimicked multimolecular frameworks and supramolecules as scaffolds for enzyme immobilization

Aggarwal

Ikram

2022

Biotech & Bioengineering

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“…9 Similarly, synthetic biology applications, catalysis using mixtures of enzymes, and other applications may benefit from using protein mixtures. 10,11 It is therefore necessary to characterize the interactions within the mixtures, as well as to detect issues, such as aggregation and self-association, in order to optimize such formulations.…”

Section: ■ Introductionmentioning

confidence: 99%

¹⁹F NMR as a Tool for Monitoring Individual Differentially Labeled Proteins in Complex Mixtures

Edwards

Derrick

Walle³

et al. 2018

Mol. Pharmaceutics

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The ability to monitor the behavior of individual proteins in complex mixtures has many potential uses, ranging from analysis of protein interactions in highly concentrated solutions, modeling biological fluids or the intracellular environment, to optimizing biopharmaceutical co-formulations. Differential labeling NMR approaches, which traditionally use N orC isotope incorporation during recombinant expression, are not always practical in cases when endogenous proteins are obtained from an organism, or where the expression system does not allow for efficient labeling, especially for larger proteins. This study proposes differential labeling of proteins by covalent attachment of F groups with distinct chemical shifts, giving each protein a unique spectral signature which can be monitored byF NMR without signal overlap, even in complex mixtures, and without any interfering signals from the buffer or other unlabeled components. Parameters, such as signal intensities, translational diffusion coefficients, and transverse relaxation rates, which report on the behavior of individual proteins in the mixture, can be recorded even for proteins as large as antibodies at a wide range of concentrations.

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“…3,4 Of significant interest is the development of multi-enzyme reactions which serve to combine the advantageous traits of enzyme catalysis and multistage reactions affording a facile and environmentally benign means of developing complex synthetic schemes. 5,6 Although numerous examples have been reported, a rather common strategy of employing multienzymatic reactions is using oxidoreductases whereby a second enzyme can be utilized in the regeneration of a reduced cofactor. 7,8 Laccase, a benzenediol:oxygen oxidoreductase, is of specific interest due to its ability to oxidize a wide variety of substrates under very mild reaction conditions.…”

Section: Introductionmentioning

confidence: 99%

“…SEC traces of poly(catechol-alt-m-xylylenediamine) polymerized using laccase/lipase (1), micellar G3-PEO13 kDa/ laccase/lipase (2), and hydrogel G3-PEO13 kDa-G4/laccase-lipase (3). Catechol comonomer (4), and m-xylylenediamine comonomer(5). Flow rate 0.8 mL/min with 0.1% LiBr in DMSO as eluent.…”

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confidence: 99%

Unprecedented Enzymatic Synthesis of Perfectly Structured Alternating Copolymers via “Green” Reaction Cocatalyzed by Laccase and Lipase Compartmentalized within Supramolecular Complexes

Scheibel

Gitsov

2018

Biomacromolecules

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This study describes the first use of laccase–lipase enzymatic reaction for the synthesis of novel perfectly structured alternating copolymers. Initially, six types of complexing agents, linear(A)–linear(B), linear(A)–linear(B)–linear(A), linear–dendritic, dendritic–linear–dendritic, linear–hyperbranched, and hyperbranched–linear–hyperbranched amphiphilic block copolymers, are proven to significantly enhance enzyme activity of three different types of lipases - Penicillium camemberti, Candida rugosa, and Burkholderia cepacia (up to 1400%, 1700%, and 870% increase with respect to the native enzymes). The copolymerization is performed in several consecutive steps: (a) lipase and laccase are dissolved in aqueous medium at neutral pH; (b) a complexing agent is added leading to cocompartmentalization of the two enzymes within a micelle or physical network; (c) the two comonomers are introduced simultaneously to the tandem enzyme complex. The reaction proceeds in the following pathway: laccase catalyzes the oxidation of catechol to o-quinone followed by lipase comediated Michael addition of a diamine. While laccase could catalyze the entire process, addition of lipase is able to increase copolymer yield up to 30.7%. Addition of a complexing agent improves the yield further up to 67.9% (23.2% yield obtained for native laccase). Complexing agents significantly increase polymer molecular mass (M w = 130 900 vs 35 500 Da for the native enzymes reaction system). The resulting copolymers are highly fluorescent (quantum yield up to 0.733) and demonstrate pH sensitive behavior, properties that hint toward their potential as imaging agents.

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Methodological Approach for Modeling of Multienzyme in-pot Processes

Cited by 3 publications

References 6 publications

A comprehensive review on bio‐mimicked multimolecular frameworks and supramolecules as scaffolds for enzyme immobilization

A comprehensive review on bio‐mimicked multimolecular frameworks and supramolecules as scaffolds for enzyme immobilization

¹⁹F NMR as a Tool for Monitoring Individual Differentially Labeled Proteins in Complex Mixtures

Unprecedented Enzymatic Synthesis of Perfectly Structured Alternating Copolymers via “Green” Reaction Cocatalyzed by Laccase and Lipase Compartmentalized within Supramolecular Complexes

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Methodological Approach for Modeling of Multienzyme in-pot Processes

Cited by 3 publications

References 6 publications

A comprehensive review on bio‐mimicked multimolecular frameworks and supramolecules as scaffolds for enzyme immobilization

A comprehensive review on bio‐mimicked multimolecular frameworks and supramolecules as scaffolds for enzyme immobilization

19F NMR as a Tool for Monitoring Individual Differentially Labeled Proteins in Complex Mixtures

Unprecedented Enzymatic Synthesis of Perfectly Structured Alternating Copolymers via “Green” Reaction Cocatalyzed by Laccase and Lipase Compartmentalized within Supramolecular Complexes

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¹⁹F NMR as a Tool for Monitoring Individual Differentially Labeled Proteins in Complex Mixtures