Purification and properties of an endo-inulinase from an Arthrobacter sp. |
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| Authors: | Su-II Kang Yung-Jin Chang Sun-Jin Oh Su-II Kim |
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| Affiliation: | (1) Department of Agricultural Chemistry and Research Center for New Bio-materials in Agriculture, College of Agriculture and Life Sciences, Seoul National University, Suwon, Korea |
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| Abstract: | ![]()
Extracellular endo-inulinase of Arthrobacter sp. S37 was purified 63-fold, giving a single band on PAGE with activity staining. The Mr was estimated as 75 kDa by SDS-PAGE. The first 31 amino acids of the N-terminal sequence was determined. The endo-inulinase hydrolyzed inulin mainly into inulo-triose (F3), inulo-tetraose (F4) and inulo-pentaose (F5) optimally at pH 7.5 and 50°C. © Rapid Science Ltd. 1998 |
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| Keywords: | endo-inulinase inulo-oligosaccharides Arthrobacter sp. |
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