Purification and Characterization of β-Fructofuranosidase from Aspergillus japonicus TIT-KJ1

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概要

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• Aβ-fructofuranosidase (EC 3.2.1.26) was purified to homogeneity from Aspergillus japonicus TIT-KJ1. The enyme had an optimum pH for activity of 5.4 and pH stability at 7.0-8.4. The optimum temperature at pH 5.4 was 60℃. The enzyme had a molecular weight of 236,000 with two subunits and an isoelectric point of pH 4.0. The enzyme was inactivated by 5 mM Hg^<2+> and Ag^+. The enzyme had a high transfructosylating activity. Treatment of 50% (w/v) sucrose with the enzyme under optimum conditions afforded more than 55% fructooligosaccharides.

• 社団法人日本農芸化学会の論文
• 1993-11-23

著者

• Sheu Dey-chyi

  Department Of Biological Engineering Tatung Institute Of Technology

• Sheu D‐c

  Department Of Bioengineering Tatung Institute Of Technolgoy

• Duan Kow-Jen

  Department of Bioengineering, Tatung Institute of Technolgoy

• Chen Jen-Shin

  Department of Bioengineering, Tatung Institute of Technolgoy

• Duan Kow-jen

  Department Of Bioengineering Tatung Institute Of Technolgoy

• Chen Jen-shin

  Department Of Bioengineering Tatung Institute Of Technolgoy

• Sheu Dey-Chyi

  Department of Bioengineering, Tatung Institute of Technolgoy

関連論文

• Purification and Characterization of Cyclodextrin Glucanotransferase from An Alkalophilic Bacterium of Taiwan(Biological Chemistry)
• Purification and Characterization of β-Fructofuranosidase from Aspergillus japonicus TIT-KJ1
• Development of t_ and its application to evaluate very-high-gravity ethanol fermentation(BIOCHEMICAL ENGINEERING)

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