Inulase from Kluyveromyces fragilis : Studies of Yeast β-Fructofuranosidase (IV)

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A strain of Kluyvermyces fragilis produced intracellular and extracellular inulases, both of which showed high activities toward inulin compared with the enzymes of Saccharomyces cerevisiae, Candida utilis and Candida kefyr. The intracellular and the extracellular enzymes from Kluyveromyces fragilis were precipitated with tannic acid and further purified on a DEAE-Sephadex A-50 column. Purification of the intracellular and extracellular enzymes afforded respectively a 42-fold and 37-fold increase in activity per mg protein and a 203-fold and 119-fold increase per mg carbohydrate. At each step of the purification, there was little change in the ration of the activities toward sucrose and inulin. Both enzymes completely digested inulin, but had no hydrolytic activities on melezitose. The enzymes had generally similar enzymatic properties, but the intracellular enzyme was more labile to urea, guanidine hydrochloride, and sodium dodecyl sulfate than the extracellular one. Both inulases were inhibited by silver nitrate, mercuric chloride, phenylhydrazine, and p-chloromercuribenzoate.
公益社団法人日本生物工学会の論文
1978-04-25