| Title : Activity and enantioselectivity of wildtype and lid mutated Candida rugosa lipase isoform 1 in organic solvents - Secundo_2004_Biotechnol.Bioeng_86_236 |
| Author(s) : Secundo F , Carrea G , Tarabiono C , Brocca S , Lotti M , Lotti Marina |
| Ref : Biotechnol Bioeng , 86 :236 , 2004 |
| Abstract : The activity and enantioselectivity of lipase 1 from Candida rugosa and of a chimera enzyme obtained by replacing the lid of isoform 1 with the lid of isoform 3 were compared in organic solvents. The alcoholysis of chloro ethyl 2-hydroxy hexanoate with methanol and of vinyl acetate with 6-methyl-5-hepten-2-ol were used as model reactions in different reaction conditions. The chimera enzyme was less active and enantioselective than the wildtype in all the conditions tested. A rationale for such decreases could be that the chimera lipase has a lower proportion of enzyme molecules in the open form. This might lead to a hindered access to the enzyme active site, thus affecting the catalytic activity. |
| ESTHER : Secundo_2004_Biotechnol.Bioeng_86_236 |
| PubMedSearch : Secundo_2004_Biotechnol.Bioeng_86_236 |
| PubMedID: 15052644 |
Secundo F, Carrea G, Tarabiono C, Brocca S, Lotti M, Lotti Marina (2004)
Activity and enantioselectivity of wildtype and lid mutated Candida rugosa lipase isoform 1 in organic solvents
Biotechnol Bioeng
86 :236
Secundo F, Carrea G, Tarabiono C, Brocca S, Lotti M, Lotti Marina (2004)
Biotechnol Bioeng
86 :236