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Title: Oscillatory behavior of US -galactosidase enzyme activity in Escherichia coli during perturbed batch experiments

Abstract

The behaviour of a wild-type and mutant strain of Escherichia coli under batch aerobic conditions were studied. In these experiments the bacteria were initially grown with lactose as the sole carbon source. When exponential growth on lactose was achieved, the batch was perturbed with D-glucose. Periodic off-line samples were taken from the fermentor and analyzed for US -galactosidase enzyme activity, D-glucose, and lactose. Continuous on-line measurements of optical density of fermentation media were also made. Oscillations in the measured enzyme activity were observed. Oscillatory behavior of US -galactosidase enzyme in E. coli was previously reported by Knorre. In his study cells were grown in D-glucose, washed, and then grown on lactose. Oscillations were attributed to the varying enzyme synthesis rate. In the present study the cells were grown initally on lactose, thus assuring high synthesis rates of US -galactosidase from the start. The oscillations observed after perturbation with glucose are pronounced and appear to be the result of combined changes in the substrate transport system and enzyme activity in addition to possible changes in enzyme synthesis rate. 10 references.

Authors:
;
Publication Date:
Research Org.:
Univ. of Delaware, Newark
OSTI Identifier:
6281430
Resource Type:
Journal Article
Journal Name:
Biotechnol. Bioeng.; (United States)
Additional Journal Information:
Journal Volume: 29:2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 09 BIOMASS FUELS; ESCHERICHIA COLI; BATCH CULTURE; ENZYME ACTIVITY; GALACTOSIDASE; BIOSYNTHESIS; AEROBIC CONDITIONS; BENCH-SCALE EXPERIMENTS; CARBON; CHEMICAL ANALYSIS; FERMENTATION; GLUCOSE; GROWTH; LACTOSE; MUTANTS; ON-LINE MEASUREMENT SYSTEMS; OPACITY; OSCILLATIONS; SAMPLING; SUBSTRATES; ALDEHYDES; BACTERIA; BIOCONVERSION; CARBOHYDRATES; DISACCHARIDES; ELEMENTS; ENZYMES; GLYCOSYL HYDROLASES; HEXOSES; HYDROLASES; MICROORGANISMS; MONOSACCHARIDES; NONMETALS; O-GLYCOSYL HYDROLASES; OLIGOSACCHARIDES; ON-LINE SYSTEMS; OPTICAL PROPERTIES; ORGANIC COMPOUNDS; PHYSICAL PROPERTIES; SACCHARIDES; SYNTHESIS; 550700* - Microbiology; 140504 - Solar Energy Conversion- Biomass Production & Conversion- (-1989)

Citation Formats

Pih, N P, and Dhurjat, P. Oscillatory behavior of US -galactosidase enzyme activity in Escherichia coli during perturbed batch experiments. United States: N. p., 1987. Web.
Pih, N P, & Dhurjat, P. Oscillatory behavior of US -galactosidase enzyme activity in Escherichia coli during perturbed batch experiments. United States.
Pih, N P, and Dhurjat, P. 1987. "Oscillatory behavior of US -galactosidase enzyme activity in Escherichia coli during perturbed batch experiments". United States.
@article{osti_6281430,
title = {Oscillatory behavior of US -galactosidase enzyme activity in Escherichia coli during perturbed batch experiments},
author = {Pih, N P and Dhurjat, P},
abstractNote = {The behaviour of a wild-type and mutant strain of Escherichia coli under batch aerobic conditions were studied. In these experiments the bacteria were initially grown with lactose as the sole carbon source. When exponential growth on lactose was achieved, the batch was perturbed with D-glucose. Periodic off-line samples were taken from the fermentor and analyzed for US -galactosidase enzyme activity, D-glucose, and lactose. Continuous on-line measurements of optical density of fermentation media were also made. Oscillations in the measured enzyme activity were observed. Oscillatory behavior of US -galactosidase enzyme in E. coli was previously reported by Knorre. In his study cells were grown in D-glucose, washed, and then grown on lactose. Oscillations were attributed to the varying enzyme synthesis rate. In the present study the cells were grown initally on lactose, thus assuring high synthesis rates of US -galactosidase from the start. The oscillations observed after perturbation with glucose are pronounced and appear to be the result of combined changes in the substrate transport system and enzyme activity in addition to possible changes in enzyme synthesis rate. 10 references.},
doi = {},
url = {https://www.osti.gov/biblio/6281430}, journal = {Biotechnol. Bioeng.; (United States)},
number = ,
volume = 29:2,
place = {United States},
year = {Thu Feb 05 00:00:00 EST 1987},
month = {Thu Feb 05 00:00:00 EST 1987}
}