BioChem - DOS

Multiple amino acid substitutions significantly improve the thermostability of feruloyl esterase A from Aspergillus niger

Bioresource technology : biomass, bioenergy, biowastes, conversion technologies, biotransformations, production technologies

Zhang, S.B.; Pei, X.Q.; Wu, Z.L.

Feruloyl esterase A from Aspergillus niger (AnFaeA) is one of the most important feruloyl esterases of industrial relevance. Previous work aided by the PoPMuSiC algorithm has identified two beneficial mutants (D93G and S187F) with thermostabilization effect. In this work, twelve additional amino acid substitutions were identified to be beneficial to the thermostability of AnFaeA after screening a random mutagenesis library constructed in Pichia pastoris. Combination of these mutations resulted in a mutant with 80% residual activity after heat treatment at 90<SUP>o</SUP>C for 15min and a half-life increasing from 15min to >4000min at 55<SUP>o</SUP>C. The thermostabilized mutant displayed significantly enhanced performance compared to the parental AnFaeA when applied to the treatment of steam-exploded corn stalk at 60<SUP>o</SUP>C together with an xylanase, demonstrating its great potential for industrial application.

2012

Elsevier Applied Science

0960-8524

117

pp.140-147

10.1016/j.biortech.2012.04.042

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART63286065

Feruloyl esterase; Aspergillus niger; Thermostability; Pichia pastoris; Directed evolution