ANCUT2, a Thermo-alkaline Cutinase from Aspergillus nidulans and Its Potential Applications
Por:
Bermudez-Garcia, Eva, Pena-Montes, Carolina, Castro-Rodriguez, Jose Augusto, Gonzalez-Canto, Augusto, Navarro-Ocana, Arturo, Farres, Amelia
Publicada:
1 jul 2017
Resumen:
Biochemical characterization of purified ANCUT2 cutinase from
Aspergillus nidulans is described. The identified amino acid sequence
differs from that predicted in Aspergillus genomic databases in amino
acids not relevant for catalysis. The enzyme is thermo-alkaline, showing
its maximum activity at pH 9 and 60 degrees C, and it retains more than
60% of its initial activity after incubation for 1 h at 60 degrees C
for pH values between 6 and 10. ANCUT2 is more active towards long-chain
esters and it hydrolyzes cutin; however, it also hydrolyzes short-chain
esters. Cutinase is inhibited by metal ions, PMSF, SDS, and EDTA (10
mM). It retains 50% of its activity in most of the solvents tested,
although it is more stable in hydrophobic solvents. According to its
found biochemical properties, preliminary assays demonstrate its ability
to synthesize methyl esters from sesame oil and the most likely
application of this enzyme remains in detergent formulations.
Filiaciones:
Univ Nacl Autonoma Mexico, Fac Quim, Dept Alimentos & Biotecnol, Ave Univ,3000 Ciudad Univ, Mexico City 04510, DF, Mexico
Univ Nacl Autonoma Mexico, Hosp Gen Mexico, Fac Med, Dept Med Expt, Dr Balmis 148, Mexico City 06726, DF, Mexico
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