Date Available

10-8-2014

Year of Publication

2014

Degree Name

Master of Science in Chemical Engineering (MSChE)

Document Type

Master's Thesis

College

Engineering

Department/School/Program

Chemical and Materials Engineering

First Advisor

Dr. Dibakar Bhattacharyya

Second Advisor

Dr. Thomas Dziubla

Abstract

While considerable progress has been made towards understanding the effect that membrane-based layer-by-layer (LbL) immobilizations have on the activity and stability of enzymatic catalysis, detailed work is required in order to fundamentally quantify and optimize the functionalization and operating conditions that define these properties. This work aims to probe deeper into the nature of transport mechanisms by use of pressure-induced, flow-driven enzymatic catalysis of LbL-functionalized hydrophilized poly(vinyldiene) (PVDF)-poly(acrylic acid) (PAA)-poly(allylamine hydrochloride) (PAH)-glucose oxidase (GOx) membranes. These membranes were coupled in a sealed series following cellulose acetate (CA) membranes for the elimination of product accumulation within the feed-side solution during operation. At pH = 6 and T = 21oC, the enzymatic catalysis of LbL-immobilized GOx from Aspergillus niger performed remarkably well in comparison to the homogeneous-phase catalysis within an analogous aqueous solution. On average, the enzymatic turnover was 0.0123 and 0.0076 mmol/(mg-GOx)(min) for the homogeneous-phase catalysis and the LbL-immobilized catalysis, respectively. Multiple consecutive permeations resulted in replicable observed kinetic results with R2 > 0.95. Permeations taking place over the course of a three week trial period resulted in a retention of >90% normalized activity when membranes were removed when not in use and stored at -20oC, whereas the homogenous-phase kinetics dropped below 90% normalized activity in under one day.

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