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

被引:0
作者
Matsunaga, Emiko [1 ]
Tanaka, Yutaka [2 ]
Toyota, Saki [1 ]
Yamada, Hisae [1 ]
Oka, Takuji [3 ]
Higuchi, Yujiro [1 ]
Takegawa, Kaoru [1 ]
机构
[1] Kyushu Univ, Fac Agr, Dept Biosci & Biotechnol, Nishi Ku, 744 Motooka, Fukuoka 8190395, Japan
[2] Tohoku Med & Pharmaceut Univ, Dept Infect & Host Def, Sendai, Miyagi 9818558, Japan
[3] Sojo Univ, Fac Biotechnol & Life Sci, Dept Appl Microbial Technol, Kumamoto 8600082, Japan
基金
日本学术振兴会;
关键词
alpha-L-Arabinofuranose; alpha-L-Arab nofuranos dase; Aspergillus fumigatus; Aspergillus nidulans; beta-D-Galactofuranose; beta-D-Galactofuranosidase; UDP-GALACTOPYRANOSE MUTASE; BIOSYNTHESIS; ROLES; NIGER; GALACTOMANNAN; GFSA;
D O I
10.1016/j.jbiosc.2020.09.066
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Although beta-D-galactofuranosidases (Galf-ases) that hydrolyze beta-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 alpha-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 beta-(1,5) and beta-(1,6) linkages, GfgA hydrolyzes beta-(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. (C) 2020, The Society for Biotechnology, Japan. All rights reserved.
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页码:1 / 7
页数:7
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