Title : Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization - Hwang_2004_Biotechnol.Lett_26_603 |
Author(s) : Hwang S , Ahn J , Lee S , Lee TG , Haam S , Lee K , Ahn IS , Jung JK |
Ref : Biotechnol Lett , 26 :603 , 2004 |
Abstract :
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. |
PubMedSearch : Hwang_2004_Biotechnol.Lett_26_603 |
PubMedID: 15168862 |
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 Lett
26 :603
Hwang S, Ahn J, Lee S, Lee TG, Haam S, Lee K, Ahn IS, Jung JK (2004)
Biotechnol Lett
26 :603