한국식품과학회지 (Korean Journal of Food Science and Technology)

한국식품과학회 (Korean Society of Food Science and Technology)
권호 표지

Pseudomonas sp.로부터 알칼리내성 amylase의 정제 및 특성 확인

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

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

두 개의 amylase를 호알칼리성 Pseudomonas sp. KFCC 10818의 배양액으로부터 정제하여 그 특성을 조사하였다. 정제된 효소의 분자량은 각각 50 kDa과 75 kDa이었다. 이 효소들의 최적반응온도는 각각 $35^{\circ}C$와 $40^{\circ}C$였으며 50 kDa의 효소는 칼슘이온에 의하여 효소활성이 두 배로 촉진되었다. 이 두 효소는 최적 pH가 6-8 부근이었으며 pH 12의 조건에서도 효소활성을 유지하는 알칼리내성을 나타냈다. Maltooligosaccharide이나 soluble starch로부터 maltose와 maltotriose를 최종 효소반응산물로 생산하였다. 두 amylase는 N-말단 아미노산 서열이 각각 QTVPKTTFV와 DTVPGNAFQ로 분석되었다.

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.

키워드

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