PURIFICATION AND CHARACTERIZATION OF BETA-FRUCTOFURANOSIDASE FROM ASPERGILLUS-JAPONICUS TIT-KJ1

被引:27
作者
DUAN, KJ
SHEU, DC
CHEN, JS
机构
[1] Department of Bioengineering, Tatung Institute of Technolgoy, Taipei 10451
关键词
D O I
10.1271/bbb.57.1811
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A beta-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-degrees-C. 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 Hg2+ 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.
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页码:1811 / 1815
页数:5
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