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KMID : 0380619770090030183
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Korean Journal of Food Science and Technology
1977 Volume.9 No. 3 p.183 ~ p.189
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Studies on the Formation of Pyridoxal Phosphate by Immobilized Cells
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유태종/Yu, Tai Jong
이택수/주영하/곡길수/Lee, Taik Soo/Chu, Young Ha/Yoshiki
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Abstract
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Studies were made of the continuous production of Pyridoxal 5´-phosphate (pyridoxal-p) on simultaneously immobilized cell column. Whole-cell of Pseudomonas polycolor having high activity of pyridoxine 5´-phosphate (pyridoxine-p) oxidase and Kloeckera sp. No. 2201 having high activity of catalase were used as the enzyme materials. The enzyme sources were entrapped in a polyacrylamide gel. Enzymatic properties of the simultaneously immobilized cells were investigated, comparing with those of the mixed whole-cells of the microorganisms. The simultaneously immobilized cells had higher enzyme activity than singly immobilized cells of Pseudomonas polycolor. From this result, the simultaneously immobilized pyridoxine-p oxidase-catalase system could be available to exert a protective effect upon the pyridoxine-p oxidase by destroying H₂O₂ which is a by-product of pyridoxine-p oxidation.
The optimum pH was 9.0 for the immobilized cells and the whole-cells. The optimum temperature was 45℃ for the immobilized cells and 40℃ for the whole-cells. The pyridoxine-p oxidase of the immobilized cells were activated by Hg^(++) and some SH-compounds.
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