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KMID : 0545119960060060402
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Journal of Microbiology and Biotechnology
1996 Volume.6 No. 6 p.402 ~ p.406
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Purification and Characterization of Inulin Fructotransferase (Depolymerizing) from Arthrobacter sp. A-6
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PARK JEONG-BOK
CHOI YONG-JIN
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Abstract
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Inulin fructotransferase (depolymerizing) (EC 2.4.1.93) was purified 34-fold from the culture broth of Arthrobacter sp. A-6 by using a combination of ammonium sulfate fractionation, DEAE-Sepharose CL-6B chromatography and Sephacryl S-200 gel filtration. The purified enzyme converts inulin into di-D-fructofuranose dianhydride Ⅲ (DFA Ⅲ) and small quantities of fructo-oligosaccharides. The temperature and pH option of the enzyme were 70℃ and 6.0, respectively. Molecular weight of the enzyme was determined to be 49 kDa by 12% SDS-polyacrylamide gel electrophoresis, and 145kDa by Sephacryl S-200 gel filtration. This indicates that the functional inulin fructotransferase of Arthrobacter sp. A-6 has a homomeric trimer structure. The enzyme had an isoeletric point of pH 4.6. The N-terminal amino acid requence of the purified enzyme subunit was Ala0Asp0Asn-Pro-Asp-Aly(?)-Ser-Asn-Met(or Glu)-Tyr-Asp-Val.
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