ScienceAsia 23 (1997): 381-388 |doi: 10.2306/scienceasia1513-1874.1997.23.381

PURIFICATION AND PROPERTIES OF CYCLODEXTRIN GLYCOSYLTRANSFERASE (CGTASE) FROM AN ALKALINE-TOLERANT BACILLUS SP. PS304

PRASERT SUNTINANALERT^a, JINTANA PETMANEECHOTE^a, NISARAT DAMNIAN^a AND NONGPORN HUTADILOK-TOWATANA^b

ABSTRACT: A cyclodextrin glycosyltransferase (CGTase) produced from Bacillus sp. PS304 was purified up to 29 folds by ammonium sulfate precipitation and DEAE-cellulose column chromatography. The purified enzyme was stable at a pH range from 4 to 12 and was most active at pH 5 and 8.5. The temperature optimum for its activity was 55^oC. The enzyme was stable up to 45 ^oC for 1 h. The isolectric point (pI) of the enzyme was 6.5. The apparent molecular weight as determined by SDS-PAGE was 76 kDa. The enzyme activity was found partially suppressed by 10 mM copper ion (Cu²⁺) and was completely inhibited in the presence of 3,4-dichloroisocoumarin at 1 mM.

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a Department of Microbiology, bDepartment of Biochemistry, Faculty of Science, Prince of Songkla University, Hatyai Campus, Songkhla 90112, Thailand.

Received 29 September 1997