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Purification and Properties of a Thermostable Inulinase (β-D-Fructan Fructohydrolase) from Bacillus stearothermophilus KP1289

✍ Scribed by Kumiko Keto; Toshihiro Araki; Tae Kitamura; Naoko Morita; Mika Moori; Yuzuru Suzuki

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 162 KB
Volume: 51
Category: Article
ISSN: 0038-9056
DOI: 10.1002/(sici)1521-379x(199907)51:7<253::aid-star253>3.0.co;2-7

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✦ Synopsis

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 constants for inulin, sucrose, and raffinose was 1:0.50:0.16. The enzyme was classified as a thermophilic thermostable β-D-fructan fructohydrolase (EC 3.2.1.80).

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## Abstract The properties of a β‐galactosidase 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