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Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases
Author(s) -
Dilokpimol Adiphol,
Verkerk Bart,
Li Xinxin,
Bellemare Annie,
Lavallee Mathieu,
Frommhagen Matthias,
Underlin Emilie Nørmølle,
Kabel Mirjam A.,
Powlowski Justin,
Tsang Adrian,
Vries Ronald P.
Publication year - 2022
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14322
Subject(s) - xylan , enzyme , esterase , biochemistry , glycoside hydrolase , chemistry , carbohydrate , substrate (aquarium) , carbohydrate binding module , biology , ecology
Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important enzymes for plant biomass degradation and are both present in Carbohydrate Esterase family 1 (CE1) of the Carbohydrate‐Active enZymes database. In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced and screened for their activity towards model and complex plant biomass substrates. CE1_1 enzymes possess AXE activity, while CE1_5 enzymes showed FAE activity. Two enzymes from CE1_2 and one from CE1_5 possess dual feruloyl/acetyl xylan esterase (FXE) activity, showing expansion of substrate specificity. The new FXEs from CE1 can efficiently release both feruloyl and acetyl residues from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation.