Continuous Production of Fructose Syrups from Inulin by Immobilized Inulinase from Aspergillus niger Mutant 817

概要

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Aspergillus niger mutant 817 was grown in submerged culture with sucrose. Inulinase was partially purified from the culture filtrate by DEAE-Cellulofine A-500 cromatography. The complex enzyme preparation containing both exo- and endoinulinases was immobilized covalently onto a porous cellulose derivative, Amino-Cellulofine, by the carbodiimide method at pH 5.0. The immobilized enzyme had 160 U inulinase activity/g (wet wt.) of the support, with the immobilization yield of 96% on a protein basis and the activity yield of 15%. The maximum inulinase activity occurred at pH 5.2 and 50℃. The immobilized enzyme was stable in the pH ranges of 4.5 to 6.5 at 30℃ and 5.0 to 6.0 at 50℃. Enzyme stability was retained up to 60℃. in a packed-bed column reactor containing 8 ml of the immobilized inulinase, a 5.0% (w/v) solution (pH 5.0) of pure dahlia inulin was completely hydrolyzed at a flow rate of 1.0 ml/min at 40℃ over a 45-d period of continuous operation. The volumetric productivity in the reactor was 410 g reducing sugars/l/h. The reaction product was a mixture of 97% D-fructose and 3% D-glucose.
社団法人日本生物工学会の論文
1995-08-25