High activity extracellular glucose (xylose) isomerase from a Chainia species |
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Authors: | M C Srinivasan H G Vartak V K Powar J M Khire |
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Institution: | (1) Biochemistry Division, National Chemical Laboratory, Pune, 411 008 Pune, India |
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Abstract: | Summary A sclerotia-forming actinomycete of the genus Chainia secreted high levels of glucose (xylose) isomerase when grown in submerged culture on a wheat bran - yeast extract medium. Maximum activity (4 units/ml) was obtained after 3–4 days when the cell bound activity was 0.19 units/ml. The two enzymes differed significantly in pH optima (extracellular, 9.5; cell-bound, 7.0) and in their adsorption behaviour on CM and DEAE celluloses. Both Mg++ and Co++ are required by the cell-bound enzyme for its optimum activity while either Mg++ or Co++ is necessary for the extracellular enzyme.NCL Communication 3320 |
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