Immobilization of Thermoanaerobium brockii alcohol dehydrogenase on SBA-15.
The activity of Thermoanaerobium brockii alcohol dehydrogenase (TBADH) adsorbed on mesoporous silica SBA-15 was compared with that of the free enzyme in water and in biphasic system (water phase up to 50% v/v water). TBADH was active at a water concentration ≥10% v/v. In the reduction reaction of sulcatone to sulcatol carried out in biphasic systems, the yield obtained with SBA-15-adsorbed TBADH was up to 5.5-fold higher than that with the free enzyme, which suggests a higher stability of the immobilized enzyme toward the organic solvent. The nature of the organic solvent substantially influenced the degree of conversion that, for example, was 7.4% in toluene and 31.6% in petroleum ether.
Istituto di Chimica del Riconoscimento Molecolare, Consiglio Nazionale delle Ricerche, via M. Bianco 9, Milan, Italy.
Michela
M
Vittorini
Emil
E
Dumitriu
Gabriel
G
Barletta
Francesco
F
Secundo
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000473:Alkanes / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D016937:Gram-Positive Endospore-Forming Rods / Q000201:enzymology*; D000442:Octanols / Q000737:chemistry; D010084:Oxidation-Reduction; D012822:Silicon Dioxide / Q000737:chemistry*; D014050:Toluene / Q000737:chemistry
D000473:Alkanes; D001426:Bacterial Proteins; D004800:Enzymes, Immobilized; D000442:Octanols; C509969:SBA-15; C009344:sulcatol; D014050:Toluene; D012822:Silicon Dioxide; D000426:Alcohol Dehydrogenase; C004544:naphtha