Abstract
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.
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Acknowledgment
The authors thank the United States Department of Agriculture: Cooperative State Research, Education and Extension Service (CSREES) (Grants 2004-35503-15220 and 2007-02134) and National Science Foundation (CBET-0653773) for supporting this work.
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McClendon, S.D., Shin, HD. & Chen, R.R. Novel bacterial ferulic acid esterase from Cellvibrio japonicus and its application in ferulic acid release and xylan hydrolysis. Biotechnol Lett 33, 47–54 (2011). https://doi.org/10.1007/s10529-010-0394-6
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DOI: https://doi.org/10.1007/s10529-010-0394-6