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    Bienzymatic Sequential Reaction on Microgel Particles and Their Cofactor Dependent Applications
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    † †Department of Nanostructured Materials, and ‡Department of Polyelectrolytes and Dispersions, Leibniz Institute of Polymer Research Dresden, Hohe Str. 6, D-01069 Dresden, Germany
    § Department of Chemistry, Technische Universität Dresden, 01069 Dresden, Germany
    ∥ College of Engineering, College of Family & Consumer Science, University of Georgia, Athens, Georgia 30602, United States
    *E-mail: [email protected]. Tel: 706-542-4885.
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    Biomacromolecules

    Cite this: Biomacromolecules 2016, 17, 5, 1610–1620
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    https://doi.org/10.1021/acs.biomac.5b01745
    Published March 24, 2016
    Copyright © 2016 American Chemical Society
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    Abstract

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    We report, the preparation and characterization of bioconjugates, wherein enzymes pyruvate kinase (Pk) and l-lactic dehydrogenase (Ldh) were covalently bound to poly(N-isopropylacrylamide)-poly(ethylenimine) (PNIPAm-PEI) microgel support using glutaraldehyde (GA) as the cross-linker. The effects of different arrangements of enzymes on the microgels were investigated for the enzymatic behavior and to obtain maximum Pk-Ldh sequential reaction. The dual enzyme bioconjugates prepared by simultaneous addition of both the enzymes immobilized on the same microgel particles (PL), and PiLi, that is, dual enzyme bioconjugate obtained by combining single-enzyme bioconjugates (immobilized pyruvate kinase (Pi) and immobilized lactate dehydrogenase (Li)), were used to study the effect of the assembly of dual enzymes systems on the microgels. The kinetic parameters (Km, kcat), reaction parameters (temperature, pH), stability (thermal and storage), and cofactor dependent applications were studied for the dual enzymes conjugates. The kinetic results indicated an improved turn over number (kcat) for PL, while the kcat and catalytic efficiency was significantly decreased in case of PiLi. For cofactor dependent application, in which the ability of ADP monitoring and ATP synthesis by the conjugates were studied, the activity of PL was found to be nearly 2-fold better than that of PiLi. These results indicated that the influence of spacing between the enzymes is an important factor in optimization of multienzyme immobilization on the support.

    Copyright © 2016 American Chemical Society

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.biomac.5b01745.

    • ATR-FTIR spectra of microgels and conjugates; plots of standardization experiments with respect to the pH, glutaraldehyde, and Pk concentration; table containing zeta potential measurements of the free and immobilized enzymes; table containing activities of conjugates prepared by sequential immobilization of enzymes; standard plot of protein concentration versus activity of Pk and Ldh; calculations for determining numbers of enzymes immobilized on single microgel particle (PDF)

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    Biomacromolecules

    Cite this: Biomacromolecules 2016, 17, 5, 1610–1620
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.biomac.5b01745
    Published March 24, 2016
    Copyright © 2016 American Chemical Society
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