Characterization of Molecular-Sieve-Bound Inulinase

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概要

• 論文の詳細を見る

• The enzyme inulinase (2,1-β-D-fructan fructanohydrolase, EC 3.2.1.7), prepared from Kluyveromyces marxianus has been immobilized using an inoranic solid support, molecular sieve 4A via the metal link method. The immobilized enzyme had around 22 units of inulinase activity per g of the support with retention of 72% of the original activity. The optimum protein to molecular sieve ration for the maximum retention of inulinase activity was 9 mg/g molecular sieve. The properties of soluble and immobilized enzyme differed in many respects. The optimum pH of the enzyme shifted from 6 to 5 and the optimum temperature of enzyme activity changed from 50 to 55℃. K_m values were 6.7 mM for soluble enzyme and 10 mM for immobilized enzyme. The heat stability of the enzyme was improved by immobilization. Immobilized enzyme retained about 76% of the original activity after 40 days of storage at room temperature (30±2℃).

• 公益社団法人日本生物工学会の論文
• 1987-04-25

著者

• MARGARITIS ARGYRIOS

  Department of Chemical and Biochemical Engineering, The University of Western Ontario

• Margaritis Argyrios

  Department Of Chemical And Biochemical Engineering The University Of Western Ontario

関連論文

• Characterization of Molecular-Sieve-Bound Inulinase
• Endocellular Fatty Acid Composition during Batch Growth and Sporulation of Bacillus thuringiensis kurstaki

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