Identification and characterization of β-D-galactofuranosidases from Aspergillus nidulans and Aspergillus fumigatus

Emiko Matsunaga, Yutaka Tanaka, Saki Toyota, Hisae Yamada, Takuji Oka, Yujiro Higuchi, Kaoru Takegawa

研究成果: Contribution to journalArticle査読

抄録

Although β-D-galactofuranosidases (Galf-ases) that hydrolyze β-D-galactofuranose (Galf)-containing oligosaccharides have been characterized in various organisms, to date no Galf-specific Galf-ase-encoding genes have been reported in Aspergillus fungi. Based on the amino acid sequences of previously identified bacterial Galf-ases, here we found two candidate Galf-specific Galf-ase genes AN2395 (gfgA) and AN3200 (gfgB) in the genome of Aspergillus nidulans. Indeed, recombinant GfgA and GfgB proteins exhibited Galf-specific Galf-ase activity, but no detectable α-L-arabinofuranosidase (Araf-ase) activity. Phylogenetic analysis of GfgA and GfgB orthologs indicated that there are two types of Aspergillus species: those containing one ortholog each for GfgA and GfgB; and those containing only one ortholog in total, among which Aspergillus fumigatus there is a representative with a single ortholog Galf-ase Afu2g14520. Unlike GfgA and GfgB, the recombinant Afu2g14520 protein showed higher Araf-ase activity than Galf-ase activity. An assay of substrate specificity revealed that although GfgA and GfgB are both exo-type Galf-ases and hydrolyze β-(1,5) and β-(1,6) linkages, GfgA hydrolyzes β-(1,6)-linked Galf-oligosaccharide more effectively as compared with GfgB. Collectively, our findings indicate that Galf-ases in Aspergillus species may have a role in cooperatively degrading Galf-containing oligosaccharides depending on environmental conditions.

本文言語英語
ページ(範囲)1-7
ページ数7
ジャーナルJournal of Bioscience and Bioengineering
131
1
DOI
出版ステータス出版済み - 1 2021

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • バイオエンジニアリング
  • 応用微生物学とバイオテクノロジー

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