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  • 标题:Fungal glycoside hydrolase family 44 xyloglucanases are restricted to the phylum Basidiomycota and show a distinct xyloglucan cleavage pattern
  • 本地全文:下载
  • 作者:Peicheng Sun ; Xinxin Li ; Adiphol Dilokpimol
  • 期刊名称:iScience
  • 印刷版ISSN:2589-0042
  • 出版年度:2022
  • 卷号:25
  • 期号:1
  • 页码:1-15
  • DOI:10.1016/j.isci.2021.103666
  • 语种:English
  • 出版社:Elsevier
  • 摘要:SummaryXyloglucan is a prominent matrix heteropolysaccharide binding to cellulose microfibrils in primary plant cell walls. Hence, the hydrolysis of xyloglucan facilitates the overall lignocellulosic biomass degradation. Xyloglucanases (XEGs) are key enzymes classified in several glycoside hydrolase (GH) families. So far, family GH44 has been shown to contain bacterial XEGs only. Detailed genome analysis revealed GH44 members in fungal species from the phylum Basidiomycota, but not in other fungi, which we hypothesized to also be XEGs. Two GH44 enzymes fromDichomitus squalensandPleurotus ostreatuswere heterologously produced and characterized. They exhibited XEG activity and displayed a hydrolytic cleavage pattern different from that observed in fungal XEGs from other GH families. Specifically, the fungal GH44 XEGs were not hindered by substitution of neighboring glucosyl units and generated various “XXXG-type,” “GXXX(G)-type,” and “XXX-type” oligosaccharides. Overall, these fungal GH44 XEGs represent a novel class of enzymes for plant biomass conversion and valorization.Graphical abstractDisplay OmittedHighlights•The fungal members of GH44 only belong to the phylum Basidiomycota•The characterized fungal GH44 xyloglucanases (XEGs) are xyloglucan-specific•These XEGs cleave xyloglucan at both sides of unsubstituted glucosyl unitsEnzymology; Mycology; Biomass
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