http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17201
Activity and enantioselectivity of wild type and lid mutated Candida rugosa lipase isoform 1 in organic solvents (Articolo in rivista)
- Type
- Label
- Activity and enantioselectivity of wild type and lid mutated Candida rugosa lipase isoform 1 in organic solvents (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/bit.20034 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Francesco Secundo; Giacomo Carrea; Chiara Tarabiono; Stefania Brocca;
Marina Lotti. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- CNR, Ist Chim Riconoscimento Mol, I-20131 Milan, Italy
Univ Milan, Dipartimento Biotecnol & Biosci, I-20126 Milan, Italy (literal)
- Titolo
- Activity and enantioselectivity of wild type and lid mutated Candida rugosa lipase isoform 1 in organic solvents (literal)
- 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. (literal)
- Prodotto di
- Autore CNR
Incoming links:
- Prodotto
- Autore CNR di
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
