Biochemical Properties of Thermostable d-Hydantoinase from Bacillus thermocatenulatus GH-2
β Scribed by JOO-HO PARK; GEUN-JOONG KIM; SEUNG-GOO LEE; HAK-SUNG KIM
- Book ID
- 111394256
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 90 KB
- Volume
- 864
- Category
- Article
- ISSN
- 0890-6564
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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 Β°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
## Abstract The properties of a Ξ²βgalactosidase from a thermophilic Bacillus have been studied and compared with the properties of the enzyme contained in whole cells and in cells entrapped in a polyacrylamide gel matrix. The partially purified enzyme appears to be optimally active at a temperature