Purification and Characterization of a Novel α-Glucuronidase from<i>Aspergillus niger</i>Specific for<i>O</i>-α-<scp>D</scp>-Glucosyluronic Acid α-<scp>D</scp>-Glucosiduronic Acid

Kiryu, Takaaki; Nakano, Hirofumi; Kiso, Taro; Murakami, Hiromi

doi:10.1271/bbb.69.522

Cited by 13 publications

(5 citation statements)

References 22 publications

(41 reference statements)

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“…The α-glucuronidase with the highest reported catalytic activity (a k cat of 202 s − 1 at 40 • C and pH 4.8) on a native substrate (aldotetraouronic acid) is from Aureobasidium pullulans [118]. Most α-glucuronidases have an optimal pH of 4.5-6.5 and an optimal temperature of 40-65 • C. There are several examples of α-glucuronidases that have acidic (pH 3-3.5) optima, but none with an alkaline optimum [119][120][121]. The α-glucuronidase from Thermotoga maritima has the highest reported temperature optimum (85 • C) [122].…”

Section: Enzymes That Catalyse Deconstruction Of Hemicellulosementioning

confidence: 99%

Plant cell walls to ethanol

Jordan

Bowman

Braker

et al. 2012

Biochemical Journal

166

112

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Conversion of plant cell walls to ethanol constitutes second generation bioethanol production. The process consists of several steps: biomass selection/genetic modification, physiochemical pretreatment, enzymatic saccharification, fermentation and separation. Ultimately, it is desirable to combine as many of the biochemical steps as possible in a single organism to achieve CBP (consolidated bioprocessing). A commercially ready CBP organism is currently unreported. Production of second generation bioethanol is hindered by economics, particularly in the cost of pretreatment (including waste management and solvent recovery), the cost of saccharification enzymes (particularly exocellulases and endocellulases displaying kcat ~1 s−1 on crystalline cellulose), and the inefficiency of co-fermentation of 5- and 6-carbon monosaccharides (owing in part to redox cofactor imbalances in Saccharomyces cerevisiae).

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Section: Enzymes That Catalyse Deconstruction Of Hemicellulosementioning

confidence: 99%

Plant cell walls to ethanol

Jordan

Bowman

Braker

et al. 2012

Biochemical Journal

166

112

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“…5b). The pH optimum of TtAguA was found to be more similar to the -glucuronidases from A. niger (Kiryu et al 2005), G. stearothermophilus (Choi et al 2000), Phanerochaete chrysosporium (Castanares et al 1995), and Bacteroides J-37 (Kim et al 1997), which have an acidic pH optima of 6.5. Conversely, the -glucuronidase from T. maritima has an optimal pH of 7.8 (Suresh et al 2002).…”

Section: Biochemical Characterizationmentioning

confidence: 85%

“…Other chemical reagents showed no noticeable influence on TtAguA. Even though the activity of the α-glucuronidase from A. niger is slightly enhanced by 2.0 mM Cu 2+ (Kiryu et al 2005), Cu 2+ inhibits most activity of TtAguA. Hence, copper reagent is used to stop the hydrolysis reaction in this study.…”

Section: +mentioning

confidence: 88%

Characterization of Thermotoga thermarum DSM 5069 α-Glucuronidase and Synergistic Degradation of Xylan

Wang

Shi

et al. 2016

BioResources

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* α-Glucuronidases are capable of breaking down the α-1,2-glycosidic bonds of 4-O-methyl-D-glucuronic acid residues. As an accessory enzyme, α-glucuronidase plays a vital role in xylan degradation. The recombinant α-glucuronidase from Thermotoga thermarum DSM 5069 was heterologously expressed in the Escherichia coli system, purified, and characterized. The purified enzyme exhibited optimal activity toward aldouronic acids at pH 6.5 and 80 °C. It was fairly thermostable and maintained 98% residual activity after incubation at 65 °C for 2.0 h. The kinetic parameters Km, Vmax, and kcat were 3.02 ± 0.16 mM, 88 ± 2 µmol min -1 mg

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“…5,6) Methyl β D glucosiduronic acid, gentiobiose dicarboxylate and cellobiose dicarboxylate were prepared by the same method from methyl β D glucoside, gentiobiose and cellobiose respectively. 5,6) New sugars, gentiobiose dicarboxylate and cellobiose dicarboxylate were identified as follows. The structure of gentiobiose dicarboxylate (β D glucosyluronic acid (1 6) D gluconic acid) was decided by NMR.…”

mentioning

confidence: 99%

“…High performance anion exchange chromatography with pulsed am- perometric detection (HPAEC PAD), TLC, NMR and MALDI TOFMS were done as described before. 6,8) Optimum pH of the enzyme was measured in 50 mM acetate buffer (pH 3.0 5.5). pH stability was measured after the enzyme was treated at 4 C for 24 h in 50 mM acetate HCl buffer (pH 1.0, 2.0), Britton Robinson buffer (pH 2.0 to 10) and glycine NaOH buffer (pH 9.0 to 12).…”

mentioning

confidence: 99%