Recombinant -glycosidases from hyperthermophilic Sulfolobus solfataricus (SsGly) and Pyrococcus furiosus (CelB) have been characterized with regard to their potential use in lactose hydrolysis at about 70°C or greater. Compared with SsGly, CelB is approximately 15 times more stable against irreve
Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable β-glycosidases and optimization of a packed-bed reactor for lactose conversion
✍ Scribed by Inge Petzelbauer; Bernhard Kuhn; Barbara Splechtna; Klaus D. Kulbe; Bernd Nidetzky
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 257 KB
- Volume
- 77
- Category
- Article
- ISSN
- 0006-3592
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Figure 2. Activation and inhibition of SsGly and CelB by D-glucose. The activity was determined in a 50 mM sodium phosphate buffer, pH 6.5, at 80°C in a 15-min long reaction, at varying concentrations of D-glucose and oNPG (᭺ SsGly, 12.5 mM oNPG; ᭹ SsGly, 22.5 mM oNPG; ᮀ CelB, 12.5 mM oNPG; CelB
During lactose conversion at 70°C, when catalyzed by -glycosidases from the archea Sulfolobus solfataricus (SsGly) and Pyrococcus furiosus (CelB), galactosyl transfer to acceptors other than water competes efficiently with complete hydrolysis of substrate. This process leads to transient formation