FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (13): 232-235.doi: 10.7506/spkx1002-6630-200913053

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Isolation, Purification and Enzymatic Characteristics of Cyclodextrin Glucanotransferase

MIN Wei-hong,DING Yin,FANG Li   

  1. College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China
  • Received:2009-04-29 Revised:2009-02-11 Online:2009-07-01 Published:2010-12-29
  • Contact: MIN Wei-hong, E-mail:minwh2000@162.com

Abstract:

The yclodextrin glucanotransferase (CGTase) produced by a high-yield CGTase-producing stain of Bacillus that isolated from soil was isolated from the fermentation broth of this strain by ammonium sulphate fractional salting out and then sequentially purified by DEAE-cellulose DE-52 ion exchange chromatography and Sephadex G-200 gel filtration chromatography. The SDS-PAGE analysis indicated that the CGTase obtained by the above procedures was of electrophoresis grade, and its molecular weight was 33 kD. The purification multiple and the recovery rate were 10 and 14.4 %, respectively. The optimum reaction temperature of the CGTase was 50 ℃, and this enzyme was stable in the range of 40—60 ℃. Its optimum reaction pH was 8.0, and it was stable in the range of pH 6.0 —10.0. The enzyme activity was strongly inhibited by Fe2+, Cu2+ and Mg2+.

Key words: Bacillus, cyclodextrin glucanotransferase, purification, enzymatic characteristics

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