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Mathematical modelling of NADH oxidation catalyzed by new NADH oxidase from Lactobacillus brevis in continuously operated enzyme membrane reactor

Paper ID Volume ID Publish Year Pages File Format Full-Text
22476 43291 2007 6 PDF Available
Title
Mathematical modelling of NADH oxidation catalyzed by new NADH oxidase from Lactobacillus brevis in continuously operated enzyme membrane reactor
Abstract

NADH oxidase from Lactobacillus brevis was kinetically characterized in two different buffers: Tris–HCl and glycine–sodium pyrophosphate (pH 9.0). Reaction kinetics was described using the Michaelis–Menten model with product (NAD+) inhibition. It was found that this type of inhibition is uncompetitive. Experiments in the continuously operated enzyme membrane reactor revealed a strong enzyme deactivation at two different residence times: 12 and 60 min. A stronger deactivation was observed at the lower residence time in the glycine–sodium pyrophosphate buffer. Enzyme deactivation was assumed to be of the first order. The developed mathematical model for the continuously operated enzyme membrane reactor described these experiments very well. The mathematical model simulations revealed that a high enzyme concentration (up to 30 g cm−3) is necessary to obtain and maintain the stationary NADH conversion near 100% for a longer period of time.

Keywords
NADH oxidase; coenzyme regeneration; enzyme kinetics; enzyme membrane reactor; inhibition
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Mathematical modelling of NADH oxidation catalyzed by new NADH oxidase from Lactobacillus brevis in continuously operated enzyme membrane reactor
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 104, Issue 4, October 2007, Pages 275–280
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Price after discount Only $4.95
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