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Updated: Aug 20, 2025

Techniques for the Evolution of Robust Pentose-fermenting Yeast for Bioconversion of Lignocellulose to Ethanol
Published on: October 24, 2016
The feruloyl esterase from Thermobacillus xylanilyticus shows broad specificity for processing pre-biotic
Carolina V Garbelotti1, Gregory S Bulmer2, Richard J Ward1
1Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, CEP 14040-901, Brazil.
Abstract:
Ferulic acid has antioxidant properties of interest to the food industry and can be released from natural plant fibres using feruloyl esterases. Esterases active at high temperatures are highly desirable but currently underrepresented. Here we report the biochemical characterization of the feruloyl esterase from Thermobacillus xylanilyticus. Specific activity of recombinant Tx-Est1 with ethyl ferulate was 29.2 ± 2.9 U mg-1, with a catalytic efficiency (Kcat/Km) of 393.7 ± 9.8 s-1mM-1. The temperature and pH optima were 60 °C and 7.5, whereby Tx-Est1 retains 70% activity after 25 h at 40 °C. MALDI-TOF MS revealed Tx-ESTI released ferulic acid from xylooligosaccharides with DP4-DP13, and from DP6-8 containing two ferulic acid groups. HPLC demonstrated ferulic acid release from destarched wheat bran was strongly potentiated by co-incubation with xylanase. These properties, especially the high activity at elevated temperatures, suggest Tx-Est1 can be employed for production of high-value compounds from agricultural waste or during plant polysaccharide saccharification.
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