Determination of the steady-state behavior of immobilized. beta. -galactosidase utilizing an integral reactor scheme

Conference · Tue Jan 01 00:00:00 EST 1985

OSTI ID:5537536

Scott, T C; Hill, Jr, C G; Amundson, C H

Analysis of the steady-state behavior of immobilized ..beta..-galactosidase by integral reactor techniques has yielded a model which allows one to predict reactor performance under normal operating conditions. Values of the mechanistic rate constants for enzymatic hydrolysis of lactose were determined as a function of temperature by fitting the reactor model to experimental lactose conversion profiles. Use of this model along with the activity decay characteristics of the immobilized enzyme which have been presented in a previous publication could prove to be a useful tool in determining appropriate operating strategies for industrial applications of the immobilized enzyme catalyst. 18 refs., 5 figs., 6 tabs.

• Research Organization: Oak Ridge National Lab., TN (USA); Wisconsin Univ., Madison (USA)
• DOE Contract Number: AC05-84OR21400
• OSTI ID: 5537536
• Report Number(s): CONF-850513-1; ON: DE85012900
• Resource Relation: Conference: Symposium on biotechnology for fuels and chemicals, Gatlinburg, TN, USA, 13 May 1985
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
BIOREACTORS
BIOCHEMICAL REACTION KINETICS
LACTOSE
ENZYMATIC HYDROLYSIS
GALACTOSIDASE
MATHEMATICAL MODELS
TEMPERATURE DEPENDENCE
CARBOHYDRATES
CHEMICAL REACTIONS
DECOMPOSITION
DISACCHARIDES
ENZYMES
GLYCOSYL HYDROLASES
HYDROLASES
HYDROLYSIS
KINETICS
LYSIS
O-GLYCOSYL HYDROLASES
OLIGOSACCHARIDES
ORGANIC COMPOUNDS
REACTION KINETICS
SACCHARIDES
SOLVOLYSIS
140504* - Solar Energy Conversion- Biomass Production & Conversion- (-1989)