Cloning and Characterization of Thermostable Endoglucanase (Cel8Y) from the Hyperthermophilic Aquifex aeolicus VF5

Kim, Jong Ok; Park, Sang Ryeol; Lim, Woo Jin; Ryu, Sung Kee; Kim, Min Keun; An, Chang Long; Cho, Soo‐Jeong; Park, Yong Woo; Kim, Jeong Hwan; Yun, Han Dae

doi:10.1006/bbrc.2000.3956

Cited by 28 publications

(5 citation statements)

References 36 publications

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“…2a), showing approximately 75% activity at 40∞C and 80∞C and less than 60% activity at a temperature above 90∞C. The optimal temperature of the enzyme was close to that previously reported from Bacillus sources, but lower than some thermophilic glucanases from thermophilic and ultra-thermophilic bacteria (Da Silva Aires et al, 2012;Kim et al, 2000;Koutsopoulos et al, 2005;Murray et al, 2001;Ueda et al, 2014). Thermostability assays (Fig.…”

Section: Characterization Of Recombinant Enzymesupporting

confidence: 84%

Expression and biochemical characterization of a multifunctional glycosidase from the thermophilic <i>Bacillus licheniformis</i> SR01

Wei

Deng

et al. 2017

J. Gen. Appl. Microbiol.

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Section: Characterization Of Recombinant Enzymesupporting

confidence: 84%

Expression and biochemical characterization of a multifunctional glycosidase from the thermophilic <i>Bacillus licheniformis</i> SR01

Wei

Deng

et al. 2017

J. Gen. Appl. Microbiol.

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“…HSH-810 (Kim et al 2005) isolated from other environments, whose endo-1,4-β-glucanases also manifest optimal activity at pH 7.0 and notable activity at a wide pH ranging from 4.5 to 10. However, these characteristics may apparently constitute an exception, because the rule is that bacterial endo-1,4-β-glucanases work at an optimal pH, but do not show activity at wide intervals of pH, as has been documented in Sporocytophaga myxococcoides (Goksoyr 1988), Pseudomonas fluorescens (Yamane et al 1970); Ruminiclostridium thermocellum (Romaniec et al 1992), Aquifex aeolicus (Kim et al 2000), Ruminococcus albus (Ohara et al 2000), Cellulomonas biazotea (Rajoka et al 2004), Clostridium cellulovorans (Arai et al 2006), Bacillus mycoides (Balasubramanian et al 2012), and Bacillus sp. (Harshvardhan et al 2013).…”

Section: Discussionmentioning

confidence: 99%

Expression, purification and characterization of an endoglucanase from Serratia proteamaculans CDBB-1961, isolated from the gut of Dendroctonus adjunctus (Coleoptera: Scolytinae)

et al. 2016

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Serratia proteamaculans CDBB-1961, a gut symbiont from the roundheaded pine beetle Dendroctonus adjunctus, displayed strong cellulolytic activity on agar-plates with carboxymethyl cellulose (CMC) as carbon source. Automatic genome annotation of S. proteamaculans made possible the identification of a single endoglucanase encoding gene, designated spr cel8A. The predicted protein, named Spr Cel8A shows high similarity (59–94 %) to endo-1,4-β-d-glucanases (EC 3.2.1.4) from the glycoside hydrolase family 8 (GH8). The gene spr cel8A has an ORF of 1113 bp, encoding a 371 amino acid residue protein (41.2 kDa) with a signal peptide of 23 amino acid residues. Expression of the gene spr cel8A in Escherichia coli yields a mature recombinant endoglucanase 39 kDa. Cel8A displayed optimal activity at pH 7.0 and 40 °C, with a specific activity of 0.85 U/mg. The enzyme was stable at pH from 4 to 8.5, retaining nearly 40–80 % of its original activity, and exhibited a half-life of 8 days at 40 °C. The Km and Vmax values for Spr Cel8A were 6.87 mg/ml and 3.5 μmol/min/mg of protein, respectively, using CMC as substrate. The final principle products of Spr Cel8A-mediated hydrolysis of CMC were cellobiose, cello oligosaccharides and a small amount of glucose, suggesting that Spr Cel8A is an endo-β-1,4-glucanase manifesting exo-activity. This is the first report regarding the functional biochemical and molecular characterization of an endoglucanase from S. proteamaculans, found in the gut-associated bacteria community of Dendroctonus bark beetles. These results contribute to improved understanding of the functional role played by this bacterium as a symbiont of bark beetles.

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“…Although the approach was successful in increasing the enzyme yield significantly, it did not have a dramatic effect on the process. Hence, we suggest the use of genetic engineering to enhance the production of this enzyme, whose applications for industrial enzymes [7], including endoglucanase cloning [4,16], are increasingly being reported. An alternate route is random mutagenesis, which historically has been proven to substantially enhance cellulase production by Trichoderma species [20].…”

Section: Discussionmentioning

confidence: 99%

Production of an endoglucanase by the shipworm bacterium, Teredinobacter turnirae

Ahuja¹,

Ferreira²,

Moreira³

2004

Journal of Industrial Microbiology and Biotechnology

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The nutritional behavior of a cellulolytic nitrogen-fixing shipworm bacterium, Teredinobacter turnirae, is described, with respect to various carbon and nitrogen sources, in terms of endoglucanase production. Also, the effects of various surfactants on enzyme production are reported. Among the carbon sources, sucrose results in the maximum enzyme production, followed by cellulose. Ammonium phosphate proves to be the best nitrogen source for endoglucanase production. Various surfactants enhance the enzyme titers, with Triton X-100 yielding the best results. A combination of the above-mentioned components improves the enzyme production by 3.6-fold.

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Cloning and Characterization of Thermostable Endoglucanase (Cel8Y) from the Hyperthermophilic Aquifex aeolicus VF5

Cited by 28 publications

References 36 publications

Expression and biochemical characterization of a multifunctional glycosidase from the thermophilic <i>Bacillus licheniformis</i> SR01

Expression and biochemical characterization of a multifunctional glycosidase from the thermophilic <i>Bacillus licheniformis</i> SR01

Expression, purification and characterization of an endoglucanase from Serratia proteamaculans CDBB-1961, isolated from the gut of Dendroctonus adjunctus (Coleoptera: Scolytinae)

Production of an endoglucanase by the shipworm bacterium, Teredinobacter turnirae

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