Activity and enantioselectivity of wildtype and lid mutated Candida rugosa lipase isoform 1 in organic solvents.
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.
Secundo
Francesco
F
Istituto di Chimica del Riconoscimento Molecolare, CNR, via Mario Bianco 9, 20131, Milano, Italy. francesco.secundo@icrm.cnr.it
Carrea
Giacomo
G
Tarabiono
Chiara
C
Brocca
Stefania
S
Lotti
Marina
M
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D002175:Candida / Q000201:enzymology*; D020134:Catalytic Domain; D004789:Enzyme Activation; D007527:Isoenzymes / Q000737:chemistry; D008049:Lipase / Q000737:chemistry*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009930:Organic Chemicals / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012997:Solvents / Q000737:chemistry*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D007527:Isoenzymes; D009930:Organic Chemicals; D011993:Recombinant Fusion Proteins; D012997:Solvents; D008049:Lipase