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Chromatographic separation and kinetic properties of fructosyltransferase from Aureobasidium pullulans

Paper ID Volume ID Publish Year Pages File Format Full-Text
24872 43542 2008 6 PDF Available
Title
Chromatographic separation and kinetic properties of fructosyltransferase from Aureobasidium pullulans
Abstract

Efficient chromatographic separation of fructosyltransferase from Aureobasidium pullulans was achieved on a preparative scale using a weak anion-exchanger Sepabeads FP-DA. The recovery yield was about 70% and the purification factor reached a value of 28. The molecular weight of the enzyme determined by size-exclusion chromatography was 570,000. The enzyme exhibited both hydrolytic and transferase activity when the latter was higher in the whole concentration range and completely dominating at higher sucrose concentrations. It was found that sucrose was the only donor of fructosyl moiety used in the transfer reaction. The initial rate method was used for the investigation of the kinetics of the action of fructosyltransferase on sucrose in the concentration range 30–2430 mM. The initial transfructosylation rate was well fitted with a linear function of the sucrose activity where the activity coefficient was an exponentially decreasing function of the sucrose concentration.

Keywords
Fructosyltransferase; Anion-exchange chromatography; Fructooligosaccharides; Enzyme purification; Kinetics; Substrate specificity
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Chromatographic separation and kinetic properties of fructosyltransferase from Aureobasidium pullulans
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 135, Issue 1, 20 May 2008, Pages 58–63
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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Any Questions? feel free to contact us