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...

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Bibliographic Details
Published in:Biotechnology letters 2011, Vol.33 (1), p.47-54
Main Authors: McClendon, Shara D, Shin, Hyun-Dong, Chen, Rachel R
Format: Article
Language:English
Subjects:
Acids
Applied Microbiology
Bacteria
Binding
Biochemistry
Biological and medical sciences
Biomass
Biomedical and Life Sciences
Biotechnology
Biotechnology - methods
Carbohydrate-binding module
Carboxylic Ester Hydrolases - chemistry
Carboxylic Ester Hydrolases - genetics
Carboxylic Ester Hydrolases - isolation & purification
Carboxylic Ester Hydrolases - metabolism
Cellvibrio - enzymology
Cloning, Molecular
Coumaric Acids - metabolism
E coli
Enzymatic activity
Enzyme Stability
Enzymes
Escherichia coli
Escherichia coli - genetics
Ferulic acid
Ferulic acid esterase
Fundamental and applied biological sciences. Psychology
Gene Expression
Genomes
Hydrogen-Ion Concentration
Hydrolysis
Life Sciences
Lignocellulose bioprocessing
Microbiology
Original Research Paper
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Sequencing
Substrates
Temperature
Xylans - metabolism
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Description
Summary: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.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-010-0394-6