Enantioselective behavior of lipases from Aspergillus niger immobilized in different supports.
Considering the extraordinary microbial diversity and importance of fungi as enzyme producers, the search for new biocatalysts with special characteristics and possible applications in biocatalysis is of great interest. Here, we report the performance in the resolution of racemic ibuprofen of a native enantioselective lipase from Aspergillus niger, free and immobilized in five types of support (Accurel EP-100, Amberlite MB-1, Celite, Montmorillonite K10 and Silica gel). Amberlite MB-1 was found to be the best support, with a conversion of 38.2%, enantiomeric excess of 50.7% and enantiomeric ratio (E value) of 19 in 72 h of reaction. After a thorough optimization of several parameters, the E value of the immobilized Aspergillus niger lipase was increased (E = 23) in a shorter reaction period (48 h) at 35 degrees C. Moreover, the immobilized Aspergillus niger lipase maintained an esterification activity of at least 80% after 8 months of storage at 4 degrees C and could be reused at least six times.
da Silva
Vania Castriani Fernandes
VC
Curso de Farmácia, Universidade São Francisco, Av. São Francisco de Assis 218, Bragança Paulista, São Paulo CEP 12916-900, Brazil.
Contesini
Fabiano Jares
FJ
de Oliveira Carvalho
Patrícia
P
D001234:Aspergillus niger / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D007052:Ibuprofen / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism*; D013237:Stereoisomerism
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D008049:Lipase; D007052:Ibuprofen