Purification and properties of a thermostable extracellular β-D-xylosidase produced by a thermotolerantAspergillus phoenicis
✍ Scribed by A C S Rizzatti; J A Jorge; H F Terenzi; C G V Rechia; M L T M Polizeli
- Book ID
- 110050829
- Publisher
- Springer-Verlag
- Year
- 2001
- Tongue
- English
- Weight
- 244 KB
- Volume
- 26
- Category
- Article
- ISSN
- 1476-5535
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Extracellular cellulolytic enzymes produced by a species of Monilia could be fractionated by chromatography on SP-Sephadex, Con A-Sepharose, and cellobiose-Sepharose. These methods did not separate the beta-D-glucosidases (beta-D-glucoside glucohydrolases, EC 3.2.1.21) from the cellulases and xylana
10 min. The enzyme released fructose exo-wise from the non-reducing end of inulin (M r = 4,5000). The Michaelis constant, catalytic center activity, and specificity constant for inulin at 60 °C and pH 5.0 were 80 mM (360 mg/mL), 460 s -1 , and 5.8 s -1 mM -1 , respectively. The ratio of specificity