Search PubMed for references concerning: FA-AraXyl2
Title: Identification and characterization of ferulic acid esterase from Penicillium chrysogenum 31B: de-esterification of ferulic acid decorated with l-arabinofuranoses and d-galactopyranoses in sugar beet pectin Phuengmaung P, Sunagawa Y, Makino Y, Kusumoto T, Handa S, Sukhumsirichart W, Sakamoto T Ref: Enzyme Microb Technol, 131:109380, 2019 : PubMed
We previously described the fungus Penicillium chrysogenum 31B, which has high performance to produce the ferulic acid esterase (FAE) for de-esterifying ferulic acids (FAs) from sugar beet pulp. However, the characteristics of this fungus have not yet been determined. Therefore, in this study, we evaluated the molecular characteristics and natural substrate specificity of the Pcfae1 gene from Penicillium chrysogenum and examined its synergistic effects on sugar beet pectin. The Pcfae1 gene was cloned and overexpressed in Pichia pastoris KM71H, and the recombinant enzyme, named PcFAE1, was characterized. The 505 amino acids of PcFAE1 possessed a GCSTG motif (Gly164 to Gly168), characteristic of the serine esterase family. By comparing the amino acid sequence of PcFAE1 with that of the FAE (AoFaeB) of Aspergillus oryzae, Ser166, Asp379, and His419 were identified as the catalytic triad. PcFAE1 was purified through two steps using anion-exchange column chromatography. Its molecular mass without the signal peptide was 75 kDa. Maximum PcFAE1 activity was achieved at pH 6.0-7.0 and 50 degreesC. The enzyme was stable up to 37 degreesC and at a pH range of 3-8. PcFAE1 activity was only inhibited by Hg(2+), and the enzyme had activity toward methyl FA, methyl caffeic acid, and methyl p-coumaric acid, with specific activities of 6.97, 4.65, and 9.32 U/mg, respectively, but not on methyl sinapinic acid. These results indicated that PcFAE1 acted similar to FaeB type according the Crepin classification. PcFAE1 de-esterified O-[6-O-feruloyl-beta-d-galactopyranosyl-(14)]-d-galactopyranose, O-[2-O-feruloyl-alpha-l-arabinofuranosyl-(15)]-l-arabinofuranose, and O-[5-O-feruloyl-alpha-l-arabinofuranosyl-(13)]-O-beta-d-xylopyranosyl-(14)-d-xylopyranose, indicating that the enzyme could de-esterify FAs decorated with both beta-d-galactopyranosidic and alpha-l-arabinofuranosidic residues in pectin and xylan. PcFAE1 acted in synergy with endo-alpha-1,5-arabinanase and alpha-l-arabinofuranosidase, which releases FA linked to arabinan, to digest the sugar beet pectin. Moreover, when PcFAE1 was allowed to act on sugar beet pectin together with Driselase, approximately 90% of total FA in the substrate was released. Therefore, PcFAE1 may be an interesting candidate for hydrolysis of lignocellulosic materials and could have applications as a tool for production of FA from natural substrates.
Title: Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger Ralet MC, Faulds CB, Williamson G, Thibault JF Ref: Carbohydr Res, 263:257, 1994 : PubMed
The activity of two forms of ferulic acid esterase (FAE) from Aspergillus niger on a synthetic feruloylated substrate (methyl ferulate) and on 11 different feruloylated oligosaccharides from sugar-beet pulp and wheat bran was determined. The enzymes exhibited different specificities for the various feruloylated substrates and were more active on certain substrates of cell-wall origin than on methyl ferulate. Both enzymes preferred the arabinose residue to which ferulic acid is attached in the furanose form. FAE-I had no clear preference for the type of linkage involved between the ferulic acid units and the oligosaccharide chain. In contrast, FAE-III had a clear requirement for ferulic acid to be attached to O-5 of the Ara f ring while no catalysis was observed when ferulic acid was attached to O-2. Both enzymes showed maximum activity on feruloylated trisaccharides. An increase in the length of the oligosaccharide chain did not preclude catalysis, but feruloylated oligosaccharides of a dp > 3 were hydrolysed at a reduced rate. Our results support the hypothesis that different kinds of ferulic acid esterases exist with different specificities for the oligosaccharide chain of the feruloylated substrates.
Title: Isolation and identification of O-(5-0-feruloyl-alpha-L-arabinofuranosyl)-1->3-O-beta-D-xylopyranosyl-(1->4)-D-xylopyranose as a component of Zea shoot cell-walls Kato Y, Navins DJ Ref: Carbohydr Res, 137:139, 1985 : PubMed
Zea shoot cell-walls were hydrolyzed with 30mm oxalic acid followed by treatment with 'Driselase'(a Basidiomycetes enzyme preparation) to obtain carbohydrate fragments containing ferulic acid. The structure of the major feruloyl compound was identified as O-(5-O-feruloyl-alpha-l-arabinofuranosyl)-(1->3)-O-beta-d-xylopyranosyl-(1->4)-d-xylopyranose on the basis of 13C-n.m.r., methylation analysis, and partial acid-hydrolysis, alkali hydrolysis, or esterase hydrolysis followed by analyses of the hydrolyzate.
