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Determination of thermodynamic data by microcalorimetry: the michaelis constant of glucose oxidase immobilized on various carriers.
Thermochim. Acta 94, 169-177 (1985)
Microcalorimetry and polarography were chosen for the investigation of dissolved and immobilized enzymes. Glucose oxidase and catalase were used bound to polyacrylamide or were immobilized by attaching them to nylon fibers which had been treated with triethyloxonium-tetrafluoroborate, diaminohexane and glutaraldehyde according to MORRIS, CAMPELL and HORNBY (1975). The latter method assured that the enzymes are located in a side chain to the polyamide structure. If, and to what degree, this immobilization could have changed the properties of the enzymes was tested by determining the MICHAELIS constant of dissolved and immobilized enzyme. Polarography, in the case of the dissolved enzymes, microcalorimetry and polarography in the case of the immobilized enzymes, led to the same Km-value. Replacement of air by oxygen increased the final heat output rate, but had no influence on the Km-value. Irradiation of the immobilized enzyme decreased the heat output rate, the Km-value remained unchanged. These results prove that once a glucose oxidase molecule is damaged it looses all activity rather than remaining partially active.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
ISSN (print) / ISBN
0040-6031
e-ISSN
0040-6031
Zeitschrift
Thermochimica Acta
Quellenangaben
Band: 94,
Heft: 1,
Seiten: 169-177
Verlag
Elsevier
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Abteilung für Strahlenbiologie und Biophysik