SUCROSE SYNTHESIS WITH IMMOBILIZED SUCROSE PHYOSPHORYLASE FROM PSEUDOMONAS SACCHAROPHILA
Abstract
The use of sucrose phosphorylase has been identified as the best and perhaps only way of synthesizing sucrose in the laboratory. With the idea of the possible eventual commercial production of synthetic sucrose in mind, the enzyme was immobilized and the properties of the immobilized enzyme were thoroughly studied. Sucrose phosphorylase was immobilized on porous ceramic beads with 3-aminopropyltriethoxysilane and glutaraldehyde. It was experimentally determined 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 kilocalories per mole. Thirteen 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. The equilibrium conversion was shifted from less than 20 percent to 30-40 percent by precipitation of phosphate as the calcium salt.
Degree
Ph.D.
Subject Area
Chemical engineering
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