Purification and characterization of beta-fructofuranosidase from Aspergillus japonicus TIT-KJ1.
A beta-fructofuranosidase (EC 3.2.1.26) was purified to homogeneity from Aspergillus japonicus TIT-KJ1. The enzyme 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.
Duan
K J
KJ
Department of Bioengineering, Tatung Institute of Technology, Taipei, Taiwan, R.O.C.
Sheu
D C
DC
Chen
J S
JS
D001230:Aspergillus / Q000201:enzymology*; D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D002473:Cell Wall / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature; D043324:beta-Fructofuranosidase
D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase