Acknowledgement
Supported by : Korea Science and Engineering Foundation(KOSEF)
Journal of Applied Biological Chemistry
- Volume 42 Issue 2
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- Pages.71-74
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- 1999
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- 1976-0442(pISSN)
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- 2234-7941(eISSN)
Isolation and Characterization of Endo-inulinases from Arthrobacter sp. S37
- Koo, Bong-Seong (Department of Agricultural Chemistry and Research Center for New Bio-Material in Agriculture, College of Agricultural and Life Science, Seoul National University) ;
- Kang, Su-Il (Department of Agricultural Chemistry and Research Center for New Bio-Material in Agriculture, College of Agricultural and Life Science, Seoul National University) ;
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Kim, Su-Il
(Department of Agricultural Chemistry and Research Center for New Bio-Material in Agriculture, College of Agricultural and Life Science, Seoul National University)
- Received : 1999.01.14
- Published : 1999.06.30
Abstract
The crude enzyme prepared from the culture supernantant of Arthrobacter sp. S37 was purified by Phenyl Toyopearl column chromatography. Six endo-inulinases were detected by activity staining on native PAGE and named Inu I to Inu VI. Endo-inulinase were further purified by DEAE cellulose column chromatography and band slicing. Inu II~VI produced mainly inulotriose (F3) and inulotetraose (F4) as well as a small amount of inulobiose (F2) and fructose in contrast to Inu I producing F3, F4 and F5 from inulin. The N-terminal amino acid sequence of native and six CNBr-cleaved fragment of Inu VI were determined. No homology was found in amino acid sequences between Inu VI and other fructan hydrolase including invertase reported.
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