Kinetics of immobilized sucrose phosphorylase

Journal Article · Mon Feb 01 04:00:00 EST 1982 · Biotechnol. Bioeng.; (United States)

DOI:https://doi.org/10.1002/bit.260240206· OSTI ID:7072023

Taylor, F; Cheng Shung Gong, L C; Tsao, G T

Sucrose phosphorylase was immobilized on porous ceramic beads with 3-aminopropyltrie-thoxysilane and glutaraldehyde. It was determined experimentally that under laboratory conditions there was no diffusional resistance to the enzyme-catalyzed reaction. The half-life of the immobilized enzyme varied from about 35 days at 30 degrees C to about 5 days at 40 degrees C. The pH optimum was found to be between 6.5 and 7.0. The activation energy for the reaction was found to be about 12.5 kcal/mol. Eleven independent kinetic constants in the complete rate equation for the previously proposed ping-pong mechanism were found to be in good agreement with those for the soluble enzyme. (Refs. 19).

• Research Organization: Lab Renewable Resources Engineering, AA Potter Engineering Centre, Purdue Univ, West Lafayette, IN 47907
• OSTI ID: 7072023
• Journal Information: Biotechnol. Bioeng.; (United States), Journal Name: Biotechnol. Bioeng.; (United States) Vol. 24:2; ISSN BIBIA
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
BENCH-SCALE EXPERIMENTS
BIOCHEMICAL REACTION KINETICS
ENZYMES
IMMOBILIZED ENZYMES
KINETICS
PH VALUE
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHOTRANSFERASES
REACTION KINETICS
SAMPLE PREPARATION
STABILITY
SUBSTRATES
TRANSFERASES