Purification, Crystallization and Some Properties of Endopolygalacturonase from Kluyveromyces fragilis
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概要
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The production of pectolytic enzyme in the genus Kluyveromyces was investigated. The production of the enzymewas dependent on the strain, and some strains belonging to K. fragilis, K. marxianus, and K. wickerhamii produced this enzyme among 11 species (29 strains) of the genus Kluyveromyces. K. fragilis IFO 0288 produced at least four endo-polygalacturonases which have different molecular weights. The dominant endo-polygalacturonase in the culture filtrate of the strain was purified and isolated as crystals. The purified enzyme was homogeneous based on analysis by polyacrylamide gel electrophoresis and ultracentrifugation. The enzyme was a glycoprotein having an isoelectric point around pH 5.6. The sedimentation coefficient (S20, w) was 3.77S, and the molecular weight was around 33, 000. The enzyme contained aspartic acid (asparagine), serine, threonine, and glycine at relatively high levels. The enzyme showed the highest activity around pH 5.0 and was stable at pH 5.0 up to 30°C. With the enzyme, and activity which releases highly polymerized pectin from various protopectins (protopectinase activity) was found.
- 社団法人 日本農芸化学会の論文
著者
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Sakai Takuo
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Yoshitake Shinobu
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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OKUSHIMA Minoru
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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