ArticleApplied and environmental microbiology2011
Three feruloyl esterases in Cellulosilyticum ruminicola H1 act synergistically to hydrolyze esterified polysaccharides.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 36 citations in OpenAlex.
- Intracellular removal of acetyl, feruloyl and p-coumaroyl decorations on arabinoxylo-oligosaccharides imported from lignocellulosic biomass degradation by Ruminiclostridium cellulolyticum.Microbial cell factories · 2024Article
- Feruloyl Esterase (International journal of molecular sciences · 2023Article
- Profiling of cool-season forage arabinoxylansFrontiers in plant science · 2023Article
- The release and catabolism of ferulic acid in plant cell wall by rumen microbes: A review.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2022Review
- Biochemical characterization of a novel feruloyl esterase from3 Biotech · 2022Article
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- Biochemical characterization of a novel thermostable feruloyl esterase from Geobacillus thermoglucosidasius DSM 2542Molecular biology reports · 2019Article
- A type D ferulic acid esterase from Streptomyces werraensis affects the volume of wheat dough pastries.Applied microbiology and biotechnology · 2018Article
- Metagenomic and metaproteomic analyses of a corn stover-adapted microbial consortium EMSD5 reveal its taxonomic and enzymatic basis for degrading lignocellulose.Biotechnology for biofuels · 2016Article
- A novel eurythermic and thermostale lipase LipM from Pseudomonas moraviensis M9 and its application in the partial hydrolysis of algal oil.BMC biotechnology · 2015Article
- Complementary symbiont contributions to plant decomposition in a fungus-farming termite.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The hemicellulolytic enzyme arsenal of Thermobacillus xylanilyticus depends on the composition of biomass used for growth.Microbial cell factories · 2012Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Feruloyl esterases (Faes) constitute a subclass of carboxyl esterases that specifically hydrolyze the ester linkages between ferulate and polysaccharides in plant cell walls. Until now, the described microbial Faes were mainly from fungi. In this study, we report that Cellulosilyticum ruminicola H1, a previously described fibrolytic rumen bacterium, possesses three different active feruloyl esterases, FaeI, FaeII, and FaeIII. Phylogenetic analysis classified the described bacterial Faes into two types, FaeI and FaeII in type I and FaeIII in type II. Substrate specificity assays indicated that FaeI is more active against the ester bonds in natural hemicelluloses and FaeIII preferentially attacks the ferulate esters with a small moiety, such as methyl groups, while FaeII is active on both types of substrates. Among the three feruloyl esterase genes, faeI was the only one induced significantly by xylose and xylan, while pectin appeared to moderately induce the three genes during the late log phase to stationary phase. Western blot analysis determined that FaeI and FaeIII were secreted and cytoplasmic proteins, respectively, whereas FaeII seemed to be cell associated. The addition of FaeI and FaeII but not FaeIII enhanced the activity of a xylanase on maize cob, suggesting a synergy of the former two with xylanase. Hence, we propose that the three feruloyl esterases work in concert to hydrolyze ferulate esters in natural hemicelluloses.
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