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Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable β-glycosidases

✍ Scribed by Inge Petzelbauer; Bernd Nidetzky; Dietmar Haltrich; Klaus D. Kulbe


Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
31 KB
Volume
65
Category
Article
ISSN
0006-3592

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✦ Synopsis


Figure 2. Activation and inhibition of Ss␤Gly 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 (᭺ Ss␤Gly, 12.5 mM oNPG; ᭹ Ss␤Gly, 22.5 mM oNPG; ᮀ CelB, 12.5 mM oNPG; CelB, 22.5 mM oNPG). V oNP,0 is the velocity of the release of oNP in the absence of added D-glucose.


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Development of an ultra-high-temperature
✍ Inge Petzelbauer; Bernd Nidetzky; Dietmar Haltrich; Klaus D. Kulbe 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 220 KB 👁 2 views

Recombinant ␤-glycosidases from hyperthermophilic Sulfolobus solfataricus (Ss␤Gly) and Pyrococcus furiosus (CelB) have been characterized with regard to their potential use in lactose hydrolysis at about 70°C or greater. Compared with Ss␤Gly, CelB is approximately 15 times more stable against irreve

Development of an ultra-high-temperature
✍ Inge Petzelbauer; Reinhard Zeleny; Andreas Reiter; Klaus D. Kulbe; Bernd Nidetzk 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 188 KB 👁 2 views

During lactose conversion at 70°C, when catalyzed by ␤-glycosidases from the archea Sulfolobus solfataricus (Ss␤Gly) and Pyrococcus furiosus (CelB), galactosyl transfer to acceptors other than water competes efficiently with complete hydrolysis of substrate. This process leads to transient formation