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Endoinulase from Streptomyces sp. S56 was immobilized by adsorption on DEAF-cellulose in 0.01 M citrate-sodium phosphate buffer, pH 6.0 and the properties of immobilized and free enzymes were investigated. The immobilized enzyme preparation, having 40 inulase activity units per dried matrix, revealed the maximal activity at pH 4.5∼5.5 and 55∼60 ℃ and were most stable at pH 6 and 45 ℃. The immobilization caused a drop in optimum pH and affinity toward inulin, a slight increase in optimum temperature, an important increase in thermal stability and maximum reaction velocity. The immobilized endoinulase hydrolyzed the tuber extract of Jerusalem artichoke and inulin, mainly into fructose and inulobise, degrading 63 and 78% of the total sugar respectively, within 48 hrs in batch reactor.
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