KMID : 0903519870300020169
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology 1987 Volume.30 No. 2 p.169 ~ p.178
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Purification and Characterization of Intracellular and Extracellular Inulase from Kluyveromyces marxianus
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Abstract
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The extracellular and intracellular inulases from Kluyveromyces marxianus were purified and characterized. The maximum production of both inulases was achieved at stationary phase in a pH-controlled medium at pH 5 with yeast nitrogen base as organic nitrogen source. Each enzyme was concentrated by tannic acid precipitation and separated into two fractions by DEAF-cellulose chromatography. Electrophoretic analysis showed that the four fractions had three glycoprotein bards each. Only main glycoprotein band, however, had both inulase and invertase activities. There were no significant differences between two enzymes in the optimum pH and temperature. But the intracellular inulases had higher heat stability and less affinity toward inuliu than the extracellular enzymes do. All the purified enzymes were considered to be exo-inulases using hydrolyzate analysis with TLC.
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