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Chemical studies of enzyme immobilization by glutaraldehyde spacing

Posted on:1988-04-25Degree:Ph.DType:Dissertation
University:Oklahoma State UniversityCandidate:Snelling, Ricky EugeneFull Text:PDF
GTID:1471390017957877Subject:Chemistry
Abstract/Summary:
Scope and method of study. Alternative enzyme reactor configurations are evaluated for their loading capacity for glutaraldehyde and two enzymes. The comparative performance of the new reactor was measured in a Flow Injection Analysis system. A method for the determination of reactive amino groups after attachment to silica surfaces is presented. The effect of solvent, temperature, reaction time, probe size and particle-pore size are investigated.;Findings and conclusions. Controlled-pore glass embedded-on-plastic reactors can be made in a few minutes, whereas the elaborate procedural steps involved in manufacturing glass capillary reactors may take as much as 3 days and utilize corrosive chemicals. The new reactors possess higher local activity, better uniformity, and desirable performance characteristics in flow systems. The analytical method presented for the determination of amino groups immobilized on silica surfaces is nondestructive and therefore of interest for in situ determination on reactor surfaces. The method involves attachment of a chromophoric probe, subsequent detachment of the immobilized probe under different experimental conditions, and final spectrophotometric measurement of the release probe at 390 nm.
Keywords/Search Tags:Method, Probe
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