Cloning, heterologous expression and biochemical characterization of a non-specific endoglucanase family 12 from Aspergillus terreus NIH2624

Segato, Fernando; Dias, Bruno Augusto; Berto, Gabriela L.; Oliveira, Dyoni Matias de; Souza, Flávio Henrique Moreira; Citadini, Ana Paula; Murakami, Mário Tyago; Damásio, André R.L.; Squina, Fábio M.; Polikarpov, Igor

doi:10.1016/j.bbapap.2017.01.003

Cited by 36 publications

(23 citation statements)

References 45 publications

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“…1c). [17] This result consistent with the observed stability of GtCel12A expressed from A. niger [19].…”

Section: Characterization Of the Gtcel12asupporting

confidence: 87%

“…In contrast, the GtCel12A expressed by A. niger has an optimal pH of 4.5, indicating N-glycosylation of the protein molecule [16,19]. Similarly, other GH12 endoglucanases from fungi have been reported to have an optimal (pH values pH 5.0-6.0) [17,27]. Optimal enzyme activity was found to occur at 50 °C within a tested range of 20-80 °C (Fig.…”

Section: Characterization Of the Gtcel12amentioning

confidence: 87%

“…However, GtCel12A exhibited notable specific activities on both substrates compared to them. [15,17,18,25,31,32].…”

Section: Characterization Of the Gtcel12amentioning

confidence: 99%

“…A variety of recombinant endoglucanases and xyloglucan-specific endoglucanases in the GH12 family have been cloned and studied using various hetero-expression hosts [14][15][16][17][18]. A G. trabeum endoglucanase expressed in a host, Aspergillus niger, has been characterized in terms of molecular weight, thermal stability, and optimal activity conditions [16,19].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of acidic endoglucanase Cel12A from Gloeophyllum trabeum and its synergistic effects on hydrogen peroxide–acetic acid (HPAC)-pretreated lignocellulose

Park

Lee

et al. 2019

J Wood Sci

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Gloeophyllum trabeum is a potent filamentous fungus that rapidly decomposes lignocellulose. In the present study, we cloned the G. trabeum cel12a gene and expressed it in Pichia pastoris strain GS115. The purified recombinant GtCel12A exhibited high pH stability and very high specific enzymic activity against β-glucan (6546 U mg −1) and carboxymethyl cellulose (1129 U mg −1) compared to GtCel5B, endoglucanases from Trichoderma reesei, and other glycoside hydrolase family 12 (GH12) enzymes. GtCel12A exhibited high enzymic activity with regard to hydrogen peroxide-acetic acid (HPAC)-pretreated lignocellulose biomass, and produced cellobiose as a major product with a small quantity of glucose. In combination with commercial cellulase, this enzyme also showed synergistic effects of 14.5, 16.1, 29.0, and 13.4% on filter paper, HPAC-pretreated pine, corn stover, and rice straw, respectively. The acidic endoglucanase GtCel12A from G. trabeum is a promising tool that can be used in combination with cellulase against HPAC-pretreated lignocellulose.

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“…1c). [17] This result consistent with the observed stability of GtCel12A expressed from A. niger [19].…”

Section: Characterization Of the Gtcel12asupporting

confidence: 87%

Section: Characterization Of the Gtcel12amentioning

confidence: 87%

“…However, GtCel12A exhibited notable specific activities on both substrates compared to them. [15,17,18,25,31,32].…”

Section: Characterization Of the Gtcel12amentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Characterization of acidic endoglucanase Cel12A from Gloeophyllum trabeum and its synergistic effects on hydrogen peroxide–acetic acid (HPAC)-pretreated lignocellulose

Park

Lee

et al. 2019

J Wood Sci

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“…The effects of metal ions on endoglucanases vary considerably. Most studies on the effects of the Cu 2+ ion have reported that it moderately or significantly inhibits purified endoglucanases (Li et al 2006;Fu et al 2010;Cheng et al 2016;Gupta et al 2017;Kanchanadumkerng et al 2017;Pimentel et al 2017;Segato et al 2017), but a few have been described enzyme activation by Cu…”

Section: Properties Of Eg-py2mentioning

confidence: 99%

A cold-active acidophilic endoglucanase of Paenibacillus sp. Y2 isolated from soil in an alpine region

Lee

Seo

et al. 2017

JABC

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A cellulolytic strain Y2 was isolated from soil obtained in the Canadian Alpine region. The isolate was identified as Paenibacillus sp. Y2 by 16S rRNA sequencing. When grown in LB medium supplemented with carboxymethyl-cellulose (CMC), CMCase production increased to 122.0% of that observed in LB without CMC. Culture supernatant was concentrated by ultrafiltration and 80% ammonium sulfate precipitates were separated by HiTrap Q and CHT-II chromatography. The purified enzyme (EG-PY2) showed a homogeneous single band and the molecular mass was estimated to be 38 kDa by SDS-PAGE. Optimum pH and temperature of the enzyme were 4.5 and 30 o C, respectively. The half-life of enzyme activity at 50 was 140.7 min, but the enzyme was drastically inactivated within 5 min at 55 , and EDTA. The enzyme was activated to 211.5% in the presence of 0.5 M of NaCl and greatly tolerant to 3.15 M of NaCl. The enzyme showed 2.98 times higher β-glucanase activity than CMCase activity. Based on these results, it can be concluded that EG-PY2 is an acidophilic, cold-active, and halotolerant endoglucanase. The authors suggest it is considered to be useful for various industrial applications, such as, fruit juice clarification, acidic deinking processes, high-salt food processing, textile and pulp industries, and for biofuel production from seaweeds.

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Optimization of biomass saccharification processes with experimental design tools for2Gethanol production: a review

Bernardi,

Gerolamo,

Dinamarco

et al. 2023

Biofuels Bioprod Bioref

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The current energy scenario has encouraged the replacement of carbon sources with renewable sources. Second‐generation (2G) ethanol production from lignocellulosic material or agroindustrial biomass involves a three‐step process consisting of pretreatment, saccharification and fermentation. Enzymatic saccharification is the most critical step for recovering fermentable sugars from biomass. Many factors such as pretreatment, enzyme load, pH, temperature, substrate and surfactant concentrations, and reaction time, among others, can affect biomass saccharification. In this sense, different design of experiment (DoE) tools together with response surface methodology (RSM) have been used as a viable strategy to determine how factors influence saccharification and to optimize this process. The strategy involves fewer experiments, less time and lower cost. This review summarizes how DoE and RSM tools have been used to optimize biomass saccharification. Moreover, an overview of the main experimental design tools used in this field is provided.

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Cloning, heterologous expression and biochemical characterization of a non-specific endoglucanase family 12 from Aspergillus terreus NIH2624

Cited by 36 publications

References 45 publications

Characterization of acidic endoglucanase Cel12A from Gloeophyllum trabeum and its synergistic effects on hydrogen peroxide–acetic acid (HPAC)-pretreated lignocellulose

Characterization of acidic endoglucanase Cel12A from Gloeophyllum trabeum and its synergistic effects on hydrogen peroxide–acetic acid (HPAC)-pretreated lignocellulose

A cold-active acidophilic endoglucanase of Paenibacillus sp. Y2 isolated from soil in an alpine region

Optimization of biomass saccharification processes with experimental design tools for2Gethanol production: a review

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