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• W2068704105 abstract "Chitinase from Bacilluslicheniformis DSM13 consists of an N-terminal catalytic domain (GH) and a C-terminal chitin binding domain (ChBD). A deletion mutant BliGH and a hybrid chitinase BliGH-CeBD were developed using polymerase chain reaction (PCR) to study the role of substrate-binding domain. Both recombinant chitinases retained their ability to bind to glycol-chitin (GC). BliGH was more effective on colloidal chitin (CC) than BliGH-CeBD as evident from the increased V(max) and k(cat) values. The fusion of CeBD improved the affinity to colloidal chitin, activity and conformational stability in BliGH-CeBD when compared with deletion mutant BliGH." @default.
• W2068704105 created "2016-06-24" @default.
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• W2068704105 date "2010-05-01" @default.
• W2068704105 modified "2023-09-27" @default.
• W2068704105 title "Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13" @default.
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• W2068704105 doi "https://doi.org/10.1016/j.biortech.2009.12.118" @default.
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