著者
Yuka Kojima Anikó Várnai Vincent G. H. Eijsink Makoto Yoshida
出版者
FCCA(Forum: Carbohydrates Coming of Age)
雑誌
Trends in Glycoscience and Glycotechnology (ISSN:09157352)
巻号頁・発行日
vol.32, no.188, pp.E135-E143, 2020-07-25 (Released:2020-07-25)
参考文献数
95
被引用文献数
3

The group of filamentous fungi called wood rotting fungi comprises the main decomposers of woody biomass in forest ecosystems. These wood rotting fungi secrete various extracellular enzymes, such as cellulases and lytic polysaccharide monooxygenases (LPMOs) to degrade cellulose in wood cell walls. Interestingly, one particular group of wood-rotting fungi, called brown-rot fungi, lacks key cellulases for degrading crystalline cellulose, namely cellobiohydrolases (CBHs), with only a few exceptions. On the other hand, genes encoding LPMOs are widely conserved among brown-rot fungi, suggesting the importance of these enzymes in the brown-rot system. In this paper, after reviewing the wood degradation process by wood rotting fungi, we describe the history of the discovery of LPMOs and then review current knowledge on the characteristics of these enzymes. We then review our research on LPMOs derived from a brown-rot fungus and discuss possible physiological roles of LPMOs in the brown-rot system. Finally, we address the significance of LPMOs in the evolution of brown-rot system.
著者
Rikako Tsukida Makoto Yoshida Satoshi Kaneko
出版者
The Japanese Society of Applied Glycoscience
雑誌
Journal of Applied Glycoscience (ISSN:13447882)
巻号頁・発行日
pp.jag.JAG-2022_0009, (Released:2022-12-26)
被引用文献数
3

Woody biomass is anticipated to be a resource for a decarbonized society, but the difficulty of isolating woody components is a significant challenge. Brown-rot fungi, a type of wood rotting fungi, decompose hemicellulose particularly efficiently. However, there are few reports on the hemicellulases from brown-rot fungi. An α-L-arabinofuranosidase belonging to glycoside hydrolase family 51 (GH51) from the brown-rot fungus Gloeophyllum trabeum (GtAbf51A) was cloned and characterized in the present study. Analyses of the phylogeny of GH51 enzymes in wood rotting fungi revealed the existence of two groups, intercellular and extracellular enzymes. After deglycosylation, the recombinant GtAbf51A produced by Pichia pastoris appeared on SDS-PAGE as approximately 71,777 daltons, which is the expected molecular weight based on the amino acid sequence of GtAbf51A. Maximum enzyme activity occurred between pH 2.2 and 4.0 and at 50°C, while it was stable between pH 2.2 and 10.0 and up to 40°C. Due to the presence of a signal peptide, GtAbf51A was thought to hydrolyze polysaccharide containing arabinose. However, the hydrolysis rate of arabinosyl linkages in polysaccharides was only 3%–4% for arabinoxylan and 17% for arabinan. GtAbf51A, in contrast, efficiently hydrolyzed arabinoxylooligosaccharides, particularly O-α-L-arabinofuranosyl-(1→3)-O-β-D-xylopyranosyl-(1→4)-β-Dxylopyranose, which is the principal product of GH10 β-xylanase. These data suggest that GtAbf51A cooperates with other xylan-degrading enzymes, such as β-xylanase, to degrade xylan in nature.
著者
Takayuki Toyama Tomotaka Kawayama Takashi Kinoshita Yohei Imamura Makoto Yoshida Koichiro Takahashi Kazuhiko Fujii Ikkou Higashimoto Tomoaki Hoshino
出版者
The Japanese Society of Internal Medicine
雑誌
Internal Medicine (ISSN:09182918)
巻号頁・発行日
pp.0488-17, (Released:2018-09-12)
参考文献数
37
被引用文献数
9

Objective This multicenter, cross-sectional, non-interventional trial aimed to investigate adherence barriers to inhaled medicines when compared with oral medicines in Japanese patients with chronic obstructive pulmonary disease (COPD) and asthma. Methods The self-reporting "Adherence Starts with Knowledge 20" (ASK-20) questionnaire was administered for adherence barriers of inhaled and oral medicines to outpatients with regular clinic attendance. Results Patients with COPD and asthma reported different adherence barriers to inhaled medicines. Independent adherence barriers (odds ratio [95% confidence interval]) to inhaled medicines relative to those for oral medicines among patients with COPD and asthma were those related to item Q8 ( "I know if I am reaching my health goals"; 2.49 [1.39-4.47]; p=0.0022) and item Q2 ( "I run out of my medicine because I do not get refills on time"; 2.69 [1.26-5.75]; p=0.0127), respectively. Among patients with poor adherence to only inhaled medicines, those with COPD and asthma recognized item Q3 ( "consuming alcohol and taking medicines"; 6.63 [1.27-34.7]; p<0.05) and item Q1 ( "forget to take medicines only sometimes"; 4.29 [1.83-10.0]; p<0.05), respectively, were recognized as independent adherence barriers to inhaled medicines. The total ASK-20 scores and total barrier counts in patients with poor adherence to inhaled medicines were significantly higher than in those without poor adherence among patients with asthma (p=0.0057) but not those with COPD (p>0.05). Conclusion These results will aid in personalizing education on adherence to inhaled medicines among patients with COPD and asthma.
著者
Yusuke Kamiyoshihara Shinji Mizuno Mirai Azuma Fumika Miyohashi Makoto Yoshida Junko Matsuno Sho Takahashi Shin Abe Hajime Shiba Keiichi Watanabe Hiroaki Inoue Akira Tateishi
出版者
The Japanese Society for Horticultural Science
雑誌
The Horticulture Journal (ISSN:21890102)
巻号頁・発行日
pp.OKD-142, (Released:2018-01-26)
被引用文献数
1

Avocado fruit ripen with ethylene production after harvest and the flesh becomes soft and edible due to degradation of cell wall polysaccharides during ripening. α-l-Arabinofuranosidase is a hydrolytic enzyme known to digest arabinose-containing cell wall polysaccharides. It has been shown that its activity increased with fruit ripening. However, our previous study showed that an α-l-arabinofuranosidase gene (PaArf/Xyl3A) is expressed in the avocado fruit before ethylene production. In addition, the transcripts were detected in some organs in which the level of ethylene was extremely low. These results indicate that the gene expression is independent of ethylene. In the present study, we carried out immunoblot analyses of α-l-arabinofuranosidase at the protein level. Using a polyclonal antibody raised against Japanese pear α-l-arabinofuranosidase, two α-l-arabinofuranosidase proteins with molecular masses of 72 kDa and 68 kDa, presumably belonging to glycoside hydrolase family 3, were detected in ripening avocado fruit. The protein levels in ethylene or 1-methylcyclopropene (1-MCP)-treated fruits were examined and the results indicated that the two proteins responded to ethylene in opposite ways; the 68 kDa protein showed a temporary accumulation, whereas the 72 kDa protein exhibited dissipation possibly caused by a loss of stability. The total enzyme activity of α-l-arabinofuranosidase was elevated faster in the ethylene-treated fruit throughout ripening and was slower in the 1-MCP-treated fruit, suggesting the existence of another α-l-arabinofuranosidase, which did not cross-react with the antibody and was positively regulated by ethylene, in ripening avocado fruit.
著者
Maki Ishiguro Tomonobu Hori Takuya Ishida Makoto Yoshida Koji Takabatake Satoshi Kaneko Kiyohiko Igarashi Masahiro Samejima
出版者
Japanese Society for Plant Biotechnology
雑誌
Plant Biotechnology (ISSN:13424580)
巻号頁・発行日
vol.27, no.3, pp.273-281, 2010-06-25 (Released:2010-07-15)
参考文献数
26
被引用文献数
5 4

The basidiomycete Flammulina velutipes is one of the most popular edible mushrooms in Japan, and has the ability to grow on cellulosic biomass as a carbon source. In this study, we have isolated two enzymes belonging to glycoside hydrolase (GH) family 7 (FvCel7A and FvCel7B) from the cellulose-grown culture of the fungus, and cloned cDNAs encoding these enzymes by utilizing a transcriptomic database of this fungus. Although both enzymes contain a catalytic domain belonging to GH family 7, only FvCel7A has the family 1 carbohydrate-binding module at the C-terminal. Sequence comparison indicated that FvCel7A and FvCel7B have a similar pattern of disulfide bonds and similar active site architecture to other fungal GH family 7 enzymes, but show small differences at loop regions covering the active site, which may affect the reactivity of cellulosic substrates.