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Two Subgroups within the GH43_36 α-l-Arabinofuranosidase Subfamily Hydrolyze Arabinosyl from Either Mono-or Disubstituted Xylosyl Units in Wheat Arabinoxylan.
Leschonski, Kai P; Kaasgaard, Svend G; Spodsberg, Nikolaj; Krogh, Kristian B R M; Kabel, Mirjam A.
Afiliación
  • Leschonski KP; Novozymes A/S, Biologiens Vej 2, 2800 Kongens Lyngby, Denmark.
  • Kaasgaard SG; Novozymes A/S, Biologiens Vej 2, 2800 Kongens Lyngby, Denmark.
  • Spodsberg N; Novozymes A/S, Biologiens Vej 2, 2800 Kongens Lyngby, Denmark.
  • Krogh KBRM; Novozymes A/S, Biologiens Vej 2, 2800 Kongens Lyngby, Denmark.
  • Kabel MA; Laboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
Int J Mol Sci ; 23(22)2022 Nov 09.
Article en En | MEDLINE | ID: mdl-36430284
Fungal arabinofuranosidases (ABFs) catalyze the hydrolysis of arabinosyl substituents (Ara) and are key in the interplay with other glycosyl hydrolases to saccharify arabinoxylans (AXs). Most characterized ABFs belong to GH51 and GH62 and are known to hydrolyze the linkage of α-(1→2)-Ara and α-(1→3)-Ara in monosubstituted xylosyl residues (Xyl) (ABF-m2,3). Nevertheless, in AX a substantial number of Xyls have two Aras (i.e., disubstituted), which are unaffected by ABFs from GH51 and GH62. To date, only two fungal enzymes have been identified (in GH43_36) that specifically release the α-(1→3)-Ara from disubstituted Xyls (ABF-d3). In our research, phylogenetic analysis of available GH43_36 sequences revealed two major clades (GH43_36a and GH43_36b) with an expected substrate specificity difference. The characterized fungal ABF-d3 enzymes aligned with GH43_36a, including the GH43_36 from Humicola insolens (HiABF43_36a). Hereto, the first fungal GH43_36b (from Talaromyces pinophilus) was cloned, purified, and characterized (TpABF43_36b). Surprisingly, TpABF43_36b was found to be active as ABF-m2,3, albeit with a relatively low rate compared to other ABFs tested, and showed minor xylanase activity. Novel specificities were also discovered for the HiABF43_36a, as it also released α-(1→2)-Ara from a disubstitution on the non-reducing end of an arabinoxylooligosaccharide (AXOS), and it was active to a lesser extent as an ABF-m2,3 towards AXOS when the Ara was on the second xylosyl from the non-reducing end. In essence, this work adds new insights into the biorefinery of agricultural residues.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Triticum / Xilanos Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: Dinamarca Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Triticum / Xilanos Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: Dinamarca Pais de publicación: Suiza