Earticle

초록

영어

Recombinant B-galactosidase from Bifidobacterium longum LL04 was expressed in Escherichia coli and partially purified by ammonium sulphate precipitation and anion-exchange chromatography (Mono-Q). The optimum temperature and pH of the partially purified enzyme were 50℃ and pH 7.0-8.0, respectively, when o-nitrophenyl-B-D-galactopyranoside was used as a substrate. The enzyme was stable over the pH range of 5.0-9.0, and was active at 40℃ for more than 60 min at pH 7.0. The enzyme was significantly activated by Na+ and K+. Maximal activity was observed at the concentration of 10 mM for both Na+ and K+. The enzyme activity was strongly inhibited by most bivalent metal ions. The Km and Vmax on ONPG at 37 and were 0.72, 167.9, and 0.507 mM, 310.9 U/mL, respectively.

목차

Abstract
 Introduction
 Materials and Methods
 Results and Discussion
 References

키워드

저자

• Lim, Seong-Il [ Division of Fermented Food Research, Korea Food Research Institute ] Corresponding author
• Kim, Geun-Bae [ Department of Animal Science and Technology, Chung-Ang University ]
• Yi, Sung-Hun [ Department of Food Science and Agricultural Chemistry, McGill University ]
• Lee, Byong-Hoon [ Department of Food Science and Agricultural Chemistry, McGill University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  Food Science and Biotechnology

• 간기

  격월간

• pISSN

  1226-7708

• 수록기간

  1992~2009

• 십진분류

  KDC 574 DDC 664