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Purification and properties of an endo-inulinase from an Arthrobacter sp.

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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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Authors and Affiliations

  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

    Su-II Kang, Yung-Jin Chang, Sun-Jin Oh & Su-II Kim

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  1. Su-II Kang
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  2. Yung-Jin Chang
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  3. Sun-Jin Oh
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  4. Su-II Kim
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Kang, SI., Chang, YJ., Oh, SJ. et al. Purification and properties of an endo-inulinase from an Arthrobacter sp.. Biotechnology Letters 20, 983–986 (1998). https://doi.org/10.1023/A:1005440910352

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  • DOI: https://doi.org/10.1023/A:1005440910352

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