Identification of the Gene Encoding Isoprimeverose-producing Oligoxyloglucan Hydrolase in Aspergillus oryzae

Matsuzawa, T.; Mitsuishi, Yasushi; Kameyama, Akihiko; Yaoi, Katsuro

doi:10.1074/jbc.m115.701474

Cited by 26 publications

(37 citation statements)

References 32 publications

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“…The xyloglucan oligosaccharides used in this study were prepared as previously described [10,14]. Their structures are shown in prepared as previously described [14] with slight modifications. Five grams of TXG was dissolved in water at a final concentration of 1% (w/v) and 1.5 mg XEG74 CD was added.…”

Section: Methodsmentioning

confidence: 99%

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Cooperation between β‐galactosidase and an isoprimeverose‐producing oligoxyloglucan hydrolase is key for xyloglucan degradation in Aspergillus oryzae

et al. 2019

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The galactosylation of xyloglucan blocks many of the enzymatic processes targeting this oligosaccharide. We found that the expression of a gene encoding Aspergillus oryzae β‐galactosidase (LacA) is induced in the presence of xyloglucan oligosaccharides. With detailed analyses of the substrate specificity of purified recombinant LacA, we show that LacA cleaves galactopyranosyl residues from xyloglucan oligosaccharides, but not from xyloglucan polysaccharide, and plays a vital role in xyloglucan degradation. LacA acts cooperatively with the isoprimeverose‐producing oligoxyloglucan hydrolase IpeA to hydrolyze xyloglucan oligosaccharides. Galactosylation of the xylopyranosyl side chain at the nonreducing end of oligoxyloglucan saccharides completely abolishes IpeA activity while LacA efficiently removes the galactopyranosyl residue. Conversely, an isoprimeverose unit at the nonreducing end of the main chain of xyloglucan oligosaccharides blocks LacA activity, while IpeA can still remove the isoprimeverose moiety. This is the first study reporting the cooperative action of β‐galactosidase and isoprimeverose‐producing oligoxyloglucan hydrolase on xyloglucan oligosaccharide degradation. Our findings shed light on the true role of LacA and the enzymatic coordination between β‐galactosidase and other hydrolases on xyloglucan degradation.

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Section: Methodsmentioning

confidence: 99%

“…The expression of the ipeA gene was induced in the presence of xyloglucan oligosaccharides. IpeA released isoprimeverose from the nonreducing end of xyloglucan oligosaccharides, but the galactosylation of xyloglucan oligosaccharides blocked IpeA activity . This implies the presence of a β‐galactosidase that is coordinated with IpeA.…”

Section: Introductionmentioning

confidence: 99%

Cooperation between β‐galactosidase and an isoprimeverose‐producing oligoxyloglucan hydrolase is key for xyloglucan degradation in Aspergillus oryzae

et al. 2019

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“…Only two IPases have been isolated, one from a bacterium ( Oerskovia sp. Y1) and the other from a eukaryote ( A. oryzae ) . The A. oryzae IPase, called IpeA, releases isoprimeverose (α‐ d ‐xylopyranosyl‐(1→6)‐ d ‐glucopyranose) units from xyloglucan oligosaccharides.…”

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confidence: 99%

“…The A. oryzae IPase, called IpeA, releases isoprimeverose (α‐ d ‐xylopyranosyl‐(1→6)‐ d ‐glucopyranose) units from xyloglucan oligosaccharides. The xylopyranose residue at the nonreducing end of xyloglucan oligosaccharide is essential for IpeA activity, and galactosylation of xylopyranose reduces IpeA activity . IPases exhibit both hydrolytic and transglycosylation activities and are able to produce di‐ and oligosaccharides .…”

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A novel isoprimeverose‐producing enzyme from Phaeoacremonium minimum is active with low concentrations of xyloglucan oligosaccharides

2018

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Xyloglucan is one of the major polysaccharides found in the plant cell wall and seeds. Owing to its complex branched structure, several different hydrolases are required to degrade it. Isoprimeverose‐producing enzymes (IPase) are unique among the glycoside hydrolase 3 family in that they recognize and release a disaccharide from the nonreducing end of xyloglucan oligosaccharides. Only two IP ases have been previously isolated and characterized. A novel IP ase from Phaeoacremonium minimum (Pm IP ase) was expressed and characterized. The xylopyranosyl residue at the nonreducing end of xyloglucan oligosaccharides was essential for hydrolytic activity, and Pm IP ase was unable to hydrolyze cellobiose into d ‐glucose. Pm IP ase had a K m for xyloglucan oligosaccharide substrate that was much lower than that of the reported IPase isolated from Aspergillus oryzae . This indicates that Pm IP ase was able to produce isoprimeverose efficiently from low concentrations of xyloglucan oligosaccharides. Pm IP ase also exhibited transglycosylation activity and was able to transfer isoprimeverose units to its substrates.

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“…34). También se describió una xylanasa de A. oryzae que libera residuos de isoprimeverosa desde xilooligosacaridos (Matsuzawa et al, 2016). Recientemente, Ishikawa et al (2018) clasificaron a este catalizador como miembro de la familia GH3.…”

Section: Análisis Filogenéticounclassified

Sistemas mono-enzimáticos de desglicosilación de flavonoides (diglicosidasas) para su aplicación en procesos tecnológicos

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Publicaciones derivadas de este trabajo de tesis 1. Publicaciones Científicas  Weiz G, Breccia JD, Mazzaferro LS. (2017). Screening and quantification of the enzymatic deglycosylation of the plant flavonoid rutin by UV-visible spectrometry. Food Chemistry. 229: 44-49.  Weiz G, Braun L, Lopez R, Domínguez de María P, Breccia JD. (2016). Enzymatic deglycosylation of flavonoids in deep eutecticsolvents-aqueous mixtures: paving the way for sustainable flavonoidchemistry. Journal of Molecular Catalysis B: Enzymatic. 130: 70-73 2. Manuscritos  Mazzaferro LS, Weiz G, Braun L, Kotik M, Pelantová H, Křen V, Breccia JD. Enzymatic rutinosylation of phenolic compounds using a fungal diglycosidase. Trabajo enviado.  Mazzaferro LS, Kotik M, Weiz G, Neher BD, Křen V, Breccia JD. Family GH5 α-L-rhamnosyl-β-D-glucosidase from Acremonium sp. DSM 24697: comparison with diglycosidases of different origin in terms of sequence and substrate specificity. Trabajo enviado.  Weiz G, Mazzaferro LS, Kotik M, Halada P, Kren V, Breccia JD. Enzymatic deglycosylation of rutin by Acremonium sp. DSM24697 fungus. (Manuscrito en preparación)

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Identification of the Gene Encoding Isoprimeverose-producing Oligoxyloglucan Hydrolase in Aspergillus oryzae

Cited by 26 publications

References 32 publications

Cooperation between β‐galactosidase and an isoprimeverose‐producing oligoxyloglucan hydrolase is key for xyloglucan degradation in Aspergillus oryzae

Cooperation between β‐galactosidase and an isoprimeverose‐producing oligoxyloglucan hydrolase is key for xyloglucan degradation in Aspergillus oryzae

A novel isoprimeverose‐producing enzyme from Phaeoacremonium minimum is active with low concentrations of xyloglucan oligosaccharides

Sistemas mono-enzimáticos de desglicosilación de flavonoides (diglicosidasas) para su aplicación en procesos tecnológicos

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