A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.
        
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Hwang S, Ahn J, Lee S, Lee TG, Haam S, Lee K, Ahn IS, Jung JK (2004) Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization Biotechnol Lett26: 603-5
Hwang S, Ahn J, Lee S, Lee TG, Haam S, Lee K, Ahn IS, Jung JK (2004) Biotechnol Lett26: 603-5