TY - JOUR
T1 - Expanding the feruloyl esterase gene family of Aspergillus niger by characterization of a feruloyl esterase, FaeC
AU - Dilokpimol, Adiphol
AU - Mäkelä, Miia R.
AU - Mansouri, Sadegh
AU - Belova, Olga
AU - Waterstraat, Martin
AU - Bunzel, Mirko
AU - de Vries, Ronald P
AU - Hildén, Kristiina S.
N1 - Publisher Copyright:
© 2017 Elsevier B.V.
PY - 2017/7/25
Y1 - 2017/7/25
N2 - A feruloyl esterase (FAE) from Aspergillus niger N402, FaeC was heterologously produced in Pichia pastoris X-33 in a yield of 10mg/L. FaeC was most active at pH 7.0 and 50°C, and showed broad substrate specificity and catalyzed the hydrolysis of methyl 3,4-dimethoxycinnamate, ethyl ferulate, methyl ferulate, methyl p-coumarate, ethyl coumarate, methyl sinapate, and methyl caffeate. The enzyme released both ferulic acid and p-coumaric acid from wheat arabinoxylan and sugar beet pectin (up to 3mg/g polysaccharide), and acted synergistically with a commercial xylanase increasing the release of ferulic acid up to six-fold. The expression of faeC increased over time in the presence of feruloylated polysaccharides. Cinnamic, syringic, caffeic, vanillic and ferulic acid induced the expression of faeC. Overall expression of faeC was very low in all tested conditions, compared to two other A. niger FAE encoding genes, faeA and faeB. Our data showed that the fae genes responded differently towards the feruloylated polysaccharides and tested monomeric phenolic compounds suggesting that the corresponding FAE isoenzymes may target different substrates in a complementary manner. This may increase the efficiency of the degradation of diverse plant biomass.
AB - A feruloyl esterase (FAE) from Aspergillus niger N402, FaeC was heterologously produced in Pichia pastoris X-33 in a yield of 10mg/L. FaeC was most active at pH 7.0 and 50°C, and showed broad substrate specificity and catalyzed the hydrolysis of methyl 3,4-dimethoxycinnamate, ethyl ferulate, methyl ferulate, methyl p-coumarate, ethyl coumarate, methyl sinapate, and methyl caffeate. The enzyme released both ferulic acid and p-coumaric acid from wheat arabinoxylan and sugar beet pectin (up to 3mg/g polysaccharide), and acted synergistically with a commercial xylanase increasing the release of ferulic acid up to six-fold. The expression of faeC increased over time in the presence of feruloylated polysaccharides. Cinnamic, syringic, caffeic, vanillic and ferulic acid induced the expression of faeC. Overall expression of faeC was very low in all tested conditions, compared to two other A. niger FAE encoding genes, faeA and faeB. Our data showed that the fae genes responded differently towards the feruloylated polysaccharides and tested monomeric phenolic compounds suggesting that the corresponding FAE isoenzymes may target different substrates in a complementary manner. This may increase the efficiency of the degradation of diverse plant biomass.
KW - Aspergillus niger
KW - Ferulic acid
KW - Feruloyl esterase
KW - Pectin
KW - Xylan
UR - http://www.scopus.com/inward/record.url?scp=85015425882&partnerID=8YFLogxK
U2 - 10.1016/j.nbt.2017.02.007
DO - 10.1016/j.nbt.2017.02.007
M3 - Article
C2 - 28285179
SN - 1871-6784
VL - 37
SP - 200
EP - 209
JO - New Biotechnology
JF - New Biotechnology
IS - Pt B
ER -