Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli |
| |
| Authors: | Federica Volontè Loredano Pollegioni Gianluca Molla Luca Frattini Flavia Marinelli Luciano Piubelli |
| |
| Affiliation: | 1.Dipartimento di Biotecnologie e Scienze Molecolari,Università degli Studi dell'Insubria via J.H. Dunant 3,Varese,Italy;2.Centro Interuniversitario di Ricerca in Biotecnologie Proteiche "The Protein Factory",Politecnico di Milano and Università degli Studi dell'Insubria,Varese,Italy |
| |
| Abstract: | Background Cholesterol oxidase is an alcohol dehydrogenase/oxidase flavoprotein that catalyzes the dehydrogenation of C(3)-OH of cholesterol. It has two major biotechnological applications, i.e. in the determination of serum (and food) cholesterol levels and as biocatalyst providing valuable intermediates for industrial steroid drug production. Cholesterol oxidases of type I are those containing the FAD cofactor tightly but not covalently bound to the protein moiety, whereas type II members contain covalently bound FAD. This is the first report on the over-expression in Escherichia coli of type II cholesterol oxidase from Brevibacterium sterolicum (BCO). |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
