Purification and Some Properties ofβ-Fructofuranosidase I from Arthrobacter sp. K-1
- 1 April 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 54 (4) , 913-919
- https://doi.org/10.1080/00021369.1990.10870051
Abstract
Arthrobacter sp. K-1, isolated from soil, produces β-fructofuranosidase. This enzyme preparation was separated into three fractions (I, II, and III) by butyl-Toyopearl 650 M column chromatography. The β-fructofuranosidase I was purified to homogeneity by disc-electrophoresis after consecutive column Chromatographies. The enzyme had a molecular weight of 52,000 by SDS-polyacrylamide gel electrophoresis and 51,000 by gel filtration with Ultrogel AcA 44, and an isoelectric point of 4.3. The enzyme was most active at pH 6.5–6.8 and at 55°C and stable up to 45°C at pH 6.5 for 30 min of incubation, and from pH 5.5 to 10.0 at 40°C in 2 hr of incubation. This enzyme hydrolyzed sucrose, erlose, raffinose, fructosylxyloside, neokestose, and stachyose at the relative velocities of 100, 75, 61, 59, 54, and 11, but hardly hydrolyzed 1-kestose and nystose (<0.02).This publication has 9 references indexed in Scilit:
- The Acceptor Specificity of Amylomaltase from Escherichia coli IFO 3806Agricultural and Biological Chemistry, 1989
- Purification and Properties of a Fructooligosaccharide-producing β-Fructofuranosidase fromAspergillus nigerATCC 20611Agricultural and Biological Chemistry, 1989
- Formation of 6-O-α-maltosylcyclomalto-oligosaccharides from α-maltosyl fluoride and cyclomalto-oligosaccharides by pullulanaseCarbohydrate Research, 1987
- Purification and characterization of invertase isozymes fromFusarium oxysporumAgricultural and Biological Chemistry, 1980
- Studies on Cyclodextrin Glycosyltransferase. IV. Enzymatic Synthesis of 3-O-α-D-Glucopyranosyl-L-sorbose and 4.O-α-D-Glucopyranosyl-D-xylose Using Cyclodextrin GlycosyltransferaseThe Journal of Biochemistry, 1976
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- Enzymically active subunits of neurospora invertaseBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
- Localization of sucrose and maltose fermenting systems in Saccharomyces cerevisiaeBiochimica et Biophysica Acta, 1962
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934