5-Hydroxymethylfurfural induces ADH7 and ARI1 expression in tolerant industrial Saccharomyces cerevisiae strain P6H9 during bioethanol production

Sehnem, Nicole Teixeira; Machado, Angela da Silva; Leite, Fernanda Cristina Bezerra; Pita, Will de Barros; Morais, Marcos Antônio de; Ayub, Marco Antônio Záchia

doi:10.1016/j.biortech.2013.01.063

Cited by 36 publications

(27 citation statements)

References 33 publications

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“…Overexpression of the dehydrogenase/reductase genes ADH6 , ADH7 , ARI1 and ALD6 increased enzyme activities for furfural and/or HMF reduction and concomitantly improved the tolerability of the host S. cerevisiae strains towards the inhibitors (Petersson et al ., ; Liu et al ., ; Liu and Moon, ; Park et al ., ). Consistent with those results, the expression levels of some dehydrogenase/reductase genes, such as ADH6 , ADH7 and ARI1 , showed much higher expression levels in the evolved inhibitor‐tolerant S. cerevisiae strains (Heer et al ., ; Liu et al ., ; Sehnem et al ., ).…”

Section: Introductionmentioning

confidence: 99%

YNL134C from Saccharomyces cerevisiae encodes a novel protein with aldehyde reductase activity for detoxification of furfural derived from lignocellulosic biomass

Zhao

Tang

Wang

et al. 2015

Yeast

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Furfural and 5-hydroxymethylfurfural (HMF) are the two main aldehyde compounds derived from pentoses and hexoses, respectively, during lignocellulosic biomass pretreatment. These two compounds inhibit microbial growth and interfere with subsequent alcohol fermentation. Saccharomyces cerevisiae has the in situ ability to detoxify furfural and HMF to the less toxic 2-furanmethanol (FM) and furan-2,5-dimethanol (FDM), respectively. Herein, we report that an uncharacterized gene, YNL134C, was highly up-regulated under furfural or HMF stress and Yap1p and Msn2/4p transcription factors likely controlled its up-regulated expression. Enzyme activity assays showed that YNL134C is an NADH-dependent aldehyde reductase, which plays a role in detoxification of furfural to FM. However, no NADH-or NADPH-dependent enzyme activity was observed for detoxification of HMF to FDM. This enzyme did not catalyse the reverse reaction of FM to furfural or FDM to HMF. Further studies showed that YNL134C is a broad-substrate aldehyde reductase, which can reduce multiple aldehydes to their corresponding alcohols. Although YNL134C is grouped into the quinone oxidoreductase family, no quinone reductase activity was observed using 1,2-naphthoquinone or 9,10-phenanthrenequinone as a substrate, and phylogenetic analysis indicates that it is genetically distant to quinone reductases. Proteins similar to YNL134C in sequence from S. cerevisiae and other microorganisms were phylogenetically analysed.

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Section: Introductionmentioning

confidence: 99%

YNL134C from Saccharomyces cerevisiae encodes a novel protein with aldehyde reductase activity for detoxification of furfural derived from lignocellulosic biomass

Zhao

Tang

Wang

et al. 2015

Yeast

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“…In S. cerevisiae , it has been shown that adaptation was at least partially due to an induction of alcohol dehydrogenases. A furfural concentration of 2 g/L induced an ADH activity increase by 78% in 48 H ; in another study, increased ADH transcription in response to exposure to 5‐hydroxymethylfurfural has been described . Therefore, we investigated transcription of ADH genes in adapted and nonadapted cells.…”

Section: Discussionmentioning

confidence: 94%

“…Adaptation of S. cerevisiae to lignocellulose by cultivation in medium containing furfural in batch , fed‐batch , and continuous culture has previously been reported. In a recent study, we showed adaptation of D. bruxellensis to lignocellulose .…”

Section: Discussionmentioning

confidence: 98%

Adaptation of Dekkera bruxellensis to lignocellulose‐based substrate

Tiukova

Pita

Sundell

et al. 2014

Biotech and App Biochem

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Adaptation of Dekkera bruxellensis to lignocellulose hydrolysate was investigated. Cells of D. bruxellensis were grown for 72 and 192 H in batch and continuous culture, respectively (adapted cells). Cultivations in semisynthetic medium were run as controls (nonadapted cells). To test the adaptation, cells from these cultures were reinoculated in the lignocellulose medium, and growth and ethanol production characteristics were monitored. Cells adapted to lignocellulose hydrolysate had a shorter lag phase, grew faster, and produced a higher ethanol concentration as compared with nonadapted cells. A stability test showed that after cultivation in rich medium, cells partially lost the adapted phenotype but still showed faster growth and higher ethanol production as compared with nonadapted cells. Because alcohol dehydrogenase genes have been described to be involved in the adaptation to furfural in Saccharomyces cerevisiae, an analogous mechanism of adaptation to lignocelluloses hydrolysate of D. bruxellensis was hypothesized. However, gene expression analysis showed that genes homologous to S. cerevisiae ADH1 were not involved in the adaptation to lignocelluloses hydrolysate in D. bruxellensis.

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“…Effect of Chlortetracycline on Ammonia Removal.T h e limiting factor of alkalinity on nitrification was excluded by maintaining an alkalinity and nitrogen ratio of 9.46 in all nitrification experiments (Jin et al, 2015;Sehnem et al, 2013). In contrast to the COD removal rate, the effect of chlortetracycline on alkalinity was not significant (p .…”

Section: Resultsmentioning

confidence: 99%

Acute Impact of Chlortetracycline on Nitrifying and Denitrifying Processes

Pulicharla

Zolfaghari²,

Brar³

et al. 2018

Water Environment Research

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In the current study, sequential nitrification and anoxic experiments in synthetic municipal wastewater were exposed to 0.5 to 100 mg/L of chlortetracycline for 24 h to evaluate acute impact on the nitrification, and denitrification processes of biological treatment. Both processes were significantly (p < 0.05) inhibited at >50 mg/L of chlortetracycline, and the results revealed that nitrification was adversely affected by chlortetracycline compared with the anoxic process. In nitrification, chemical oxygen removal (COD) and ammonia oxidation kinetics were 50% inhibited at 10 mg chlortetracycline/L, and nitrite oxidation kinetics at 0.5 mg chlortetracycline/L. Likewise, in the anoxic process, 14 and 10 mg/L of chlortetracycline inhibited 50% of COD removal and nitrate reduction kinetics, respectively. In nitrification and denitrification, 90% of chlortetracycline was removed by adsorbing onto sludge suspended solids. In addition, a higher chlortetracycline concentration in anoxic effluent, compared with aerobic effluents, indicated a dissimilarity in the composition of sludge solids, pH, and biomass production for both processes.

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5-Hydroxymethylfurfural induces ADH7 and ARI1 expression in tolerant industrial Saccharomyces cerevisiae strain P6H9 during bioethanol production

Cited by 36 publications

References 33 publications

YNL134C from Saccharomyces cerevisiae encodes a novel protein with aldehyde reductase activity for detoxification of furfural derived from lignocellulosic biomass

YNL134C from Saccharomyces cerevisiae encodes a novel protein with aldehyde reductase activity for detoxification of furfural derived from lignocellulosic biomass

Adaptation of Dekkera bruxellensis to lignocellulose‐based substrate

Acute Impact of Chlortetracycline on Nitrifying and Denitrifying Processes

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