Purification and Characterization of Alkali-resistant Amylases from Pseudomonas sp.

Pseudomonas sp.로부터 알칼리내성 amylase의 정제 및 특성 확인

  • Lee, Jeong-Eun (Department of Food and Nutrition, Chonnam National University) ;
  • Jhon, Deok-Young (Department of Food and Nutrition, Chonnam National University)
  • 이정은 (전남대학교 식품영양학과) ;
  • 전덕영 (전남대학교 식품영양학과)
  • Published : 2008.02.28

Abstract

Two extracellular amylase isozymes were purified and characterized from alkalophilic Pseudomonas sp. KFCC 10818 for the production of maltooligosaccharides. The molecular weights of the homogeneous proteins were 50 kDa and 75 kDa, respectively. The 50 and 75 kDa amylases showed optimum temperatures at 35 and $40^{\circ}C$, respectively. The optimum pH of the enzymes ranged from pH 6-8, and the enzymes were resistant to an alkaline condition of pH 12. Via the enzyme's actions, the final products from maltooligosaccharides or soluble starch were maltose and maltotriose. Calcium was a potent activator of the 50 kDa amylase. Finally, the N-terminal amino acid sequences of the 50 and 75 kDa amylases were QTVPKTTFV and DTVPGNAFQ, respectively.

Keywords

amylase;purification;N-terminal sequencing;Pseudomonas sp.

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