Novel bacterial ferulic acid esterase from Cellvibrio japonicus and its application in ferulic acid release and xylan hydrolysis.
Recent genome sequencing of Cellvibrio japonicas revealed the presence of two highly homologous ferulic acid esterases (FAEs), encoded by fee1A and fee1B. In this work, the putative FAE, Fee1B, was successfully cloned and expressed in an E. coli system and the purified enzyme was characterized as a type-D FAE with a pH and temperature optima of 6.5 and 35-40°C, respectively. Additionally, the two tandem N-terminal carbohydrate binding modules of the multi-domain enzyme were shown to be crucial for optimum enzyme activity. The potential of the enzyme in biomass processing was demonstrated with its high synergy with a xylanase in the release of reducing sugar from arabinoxylan and its ability to liberate ferulic acid from various complex xylan substrates.
McClendon
Shara D
SD
School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA 30332-0100, USA.
Shin
Hyun-Dong
HD
Chen
Rachel R
RR
D018533:Biomass; D001709:Biotechnology / Q000379:methods; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D020633:Cellvibrio / Q000201:enzymology*; D003001:Cloning, Molecular; D003373:Coumaric Acids / Q000378:metabolism*; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013696:Temperature; D014990:Xylans / Q000378:metabolism*
D003373:Coumaric Acids; D011994:Recombinant Proteins; D014990:Xylans; C004999:ferulic acid; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase