Evaluation of Polycation-Stabilized Lactate Oxidase in a Silica Sol–Gel as a Biosensor Platform |
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Authors: | James A Cox Patrick M Hensley Cheryl L Loch |
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Institution: | (1) Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA, US |
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Abstract: | Whereas glucose oxidase and related proteins are encapsulated readily in silica sol–gels, α-hydroxy enzymes such as lactate
oxidase (LOx), are reported to be damaged by electrostatic interaction with these matrices. Based on a previous report, poly(ethyleneimine),
PEI, was evaluated as a protecting compound under conditions suited to analytical measurements. With LOx and PEI co-encapsulated
in a silica sol–gel, the enzyme retained 62% of its initial activity after 20 days. In the absence of PEI, activity was lost
during the processing. Batch analytical measurements with enzyme-doped sol–gel yielded a linear response over the range 0.5–2.0 mM
lactate and a detection limit of 0.03 mM lactate. Both simple incorporation of LOx in a silica sol–gel and an alternative
protection method, blocking the ion-exchange sites on silica with La(III), failed. These negative results supported the hypothesis
that the efficacy of PEI was related to its formation of a protective sheath around the enzyme.
Author for correspondence. E-mail: coxja@muohio.edu
Received July 29, 2002; accepted December 15, 2002
Published online May 19, 2003 |
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Keywords: | : Lactate oxidase silica sol– gel stabilization |
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