Thermostable feruloyl esterase for the bioproduction of ferulic acid from triticale bran

Abokitse, Kofi; Wu, Meiqun; Bergeron, Hélène; Große, Stephan; Lau, Peter C. K.

doi:10.1007/s00253-010-2441-6

Cited by 40 publications

(30 citation statements)

References 64 publications

(68 reference statements)

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“…Most previous studies show that it is the (hemi)cellulases that assist Faes in ferulic acid release (1,11,12,14,18,19,28,29,30); however, in the present study, we found that xylanase does not assist FaeI and FaeII in the release of ferulic acid from maize cob, except for the stimulation of FaeIII. In contrast, FaeI and FaeII, the type I bacterial Faes, rather than FaeIII, the type II bacterial Fae, promote the activity of xylanase; similar synergistic effects were also observed previously (39,44).…”

Section: Discussioncontrasting

confidence: 54%

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

Cai

Luo

et al. 2011

Appl Environ Microbiol

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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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Section: Discussioncontrasting

confidence: 54%

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

Cai

Luo

et al. 2011

Appl Environ Microbiol

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“…Feruloyl esterase, also known as cinnamoyl esterase, is an enzyme that hydrolyzes ferulate ester groups from hemicellulose molecules, which represent cross-links among hemicellulose chains and lignin polymers (218). Feruloyl esterases belong to the CE1 family and hydrolyze the ester bond between hydroxycinnamic acid and sugars present in plant cell walls (219).…”

Section: Hemicellulasesmentioning

confidence: 99%

Genomics Review of Holocellulose Deconstruction by Aspergilli

Segato

Damásio

Lucas

et al. 2014

Microbiol Mol Biol Rev

113

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SUMMARY Biomass is constructed of dense recalcitrant polymeric materials: proteins, lignin, and holocellulose, a fraction constituting fibrous cellulose wrapped in hemicellulose-pectin. Bacteria and fungi are abundant in soil and forest floors, actively recycling biomass mainly by extracting sugars from holocellulose degradation. Here we review the genome-wide contents of seven Aspergillus species and unravel hundreds of gene models encoding holocellulose-degrading enzymes. Numerous apparent gene duplications followed functional evolution, grouping similar genes into smaller coherent functional families according to specialized structural features, domain organization, biochemical activity, and genus genome distribution. Aspergilli contain about 37 cellulase gene models, clustered in two mechanistic categories: 27 hydrolyze and 10 oxidize glycosidic bonds. Within the oxidative enzymes, we found two cellobiose dehydrogenases that produce oxygen radicals utilized by eight lytic polysaccharide monooxygenases that oxidize glycosidic linkages, breaking crystalline cellulose chains and making them accessible to hydrolytic enzymes. Among the hydrolases, six cellobiohydrolases with a tunnel-like structural fold embrace single crystalline cellulose chains and cooperate at nonreducing or reducing end termini, splitting off cellobiose. Five endoglucanases group into four structural families and interact randomly and internally with cellulose through an open cleft catalytic domain, and finally, seven extracellular β-glucosidases cleave cellobiose and related oligomers into glucose. Aspergilli contain, on average, 30 hemicellulase and 7 accessory gene models, distributed among 9 distinct functional categories: the backbone-attacking enzymes xylanase, mannosidase, arabinase, and xyloglucanase, the short-side-chain-removing enzymes xylan α-1,2-glucuronidase, arabinofuranosidase, and xylosidase, and the accessory enzymes acetyl xylan and feruloyl esterases.

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“…In recent years, the available ever-increasing genomic sequences of microorganisms have significantly promoted the discovery of new catalysts [9,10]. To date, several new feruloyl esterases have been successfully identified through genome mining and heterologously expressed in Escherichia coli or Pichia pastoris, which are much more labor-and time-saving in comparison with the traditional screening method [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation

Zhang

Wang

Lü

et al. 2015

Protein Expression and Purification

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Thermostable feruloyl esterase for the bioproduction of ferulic acid from triticale bran

Cited by 40 publications

References 64 publications

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides

Genomics Review of Holocellulose Deconstruction by Aspergilli

Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation

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