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

Identification and characterization of a novel “thermophilic-like” Old Yellow Enzyme from the genome of Chryseobacterium sp. CA49

“…Such characteristic of mesophilic enzymes with excellent thermostability is usually desired because it could avoid the necessity of applying high reaction temperature when using thermophilic enzymes to reduce energy consumption, as well as to fit the thermal tolerance of other reactants, while at the same time, maintain many advantages of a stable enzyme, such as less enzyme loading, easy catalyst manipulation, and flexible process operations [42][43][44].…”

Rapid asymmetric reduction of ethyl 4-chloro-3-oxobutanoate using a thermostabilized mutant of ketoreductase ChKRED20

“…To generate more thermostable mutants of ChKRED20, we subsequently applied combinations of beneficial mutations for possible synergistic or additive effect (Giver et al 1998;Hirokawa et al 2008;McLachlan et al 2008;Pei et al 2011;Zhang et al 2012). After the generation of several double, triple, and quadruple mutants, their residual activities were measured after heat treatment at 70°C for 3 h using the crude enzyme extracts (Fig.…”

Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation

“…In recent years, feruloyl esterases have been focused as a promising biocatalyst in the fields of biofuel production, pharmaceutical synthesis and organic food making [3,4]. To date, tens of FAEs have been confirmed by screening a diversity of microorganisms, which has provided valuable information for its application and directed evolution [5,6].…”