2005
DOI: 10.1271/bbb.69.522
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Purification and Characterization of a Novel α-Glucuronidase fromAspergillus nigerSpecific forO-α-D-Glucosyluronic Acid α-D-Glucosiduronic Acid

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Cited by 15 publications
(5 citation 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%
“…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%
“…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%
“…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%