Production of levan using recombinant levansucrase immobilized on hydroxyapatite

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Production of levan using recombinant levansucrase immobilized on hydroxyapatite
Ki Hyo Jang; Ki Bang Song; J S Kim; Chul Ho Kim; Bong Hyun Chung; Sang Ki Rhee
Bibliographic Citation
Bioprocess Engineering, vol. 23, no. 1, pp. 89-93
Publication Year
Levansucrase of Zymomonas mobilis was immobilized onto the surface of hydroxyapatite by ionic binding. Optimum conditions for the immobilization were: pH 6.0, 4 h of immobilization reaction time, and 20 U of enzyme/g of matrix. The enzymatic and biochemical properties of the immobilized enzyme were similar to those of the native enzyme, especially towards the effect of salts and detergents. The immobilized enzyme showed sucrose hydrolysis activity higher as that of the native enzyme, but levan formation activity was 70% of the native enzyme. HPLC analysis of levan produced by immobilized enzyme showed the presence of two different types of levan: high-molecular-weight levan and low-molecular-weight levan. The proportion of low-molecular-weight levan to total levan produced by the immobilized enzyme was much higher than that with the native enzyme, indicating that immobilized levansucrase could be applied to produce low-molecular-weight levan. Immobilized levansucrase retained 65% of the original activity after 6 times of repeated uses and 67% of the initial activity after 40 d when stored at 4°C.
hydroxyapatitelevanlevansucraserecombinant enzyme
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Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
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