Full TGIF Record # 39848
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Web URL(s):http://www.blackwell-synergy.com/doi/pdf/10.1046/j.1469-8137.1997.00642.x
    Last checked: 02/15/2006
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Publication Type:
i
Refereed
Author(s):Marx, Stefan P.; Nösberger, Josef; Frehner, Marco
Author Affiliation:Institute of Plant Sciences, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich, Switzerland
Title:Hydrolysis of fructan in grasses: a ẞ - (2 - 6) - linkage specific fructan - ẞ - fructosidase from stubble of Lolium perenne
Source:New Phytologist. Vol. 135, No. 2, February 1997, p. 279-290.
Publishing Information:Oxford, England: Cambridge University Press.
# of Pages:12
Keywords:TIC Keywords: Temperatures; Sucrose; Fructose; Hydrolysis; Lolium perenne
Abstract/Contents:"Several different fructan and sucrose hydrolysing enzyme activities were induced in roots and stubble (mainly leaf sheaths) of Lolium perenne L. plants after defoliation. Among those activities, a fructan - ẞ - fructosidase (EC 3.2.1.80) that hydrolyses predominantly ẞ - (2 - 6) - fructosyl-fructose linkages (6-FEH) was purified from the stubble. The use of substrate 6,6-kestotetraose and high-performance anoin-exchange chromatogrography with pulsed amperometric detection allowed linkage-specific screening and sensitive analysis of enzyme activity. A 6-FEH was extensively purified to yield one protein band as revealed by one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The 6-FEH was separated from the contaminating ẞ - (2 - 1) - linkage-specific fructan-ẞ-fructosidase and invertase activities (EC 3.1.2.26) by ammonium sulphate precipitation, lectin-affinity, anion-exchange and size-exclusion chromatography. The purified 6-FEH was a glycoprotein with an apparent molecular mass of 65 000, as determined by size-exclusion chromatography, and of 69 000 by SDS-PAGE. The 6-FEH had an activity optimum in the range of pH 5 x 1 to 5 x 6. Temperatures above 30°C affected the stability of the enzyme activity; however, its temperature stability was increased in the presence of 6,6-kestotetraose. The purified 6-FEH activity hydrolysed the ẞ - (2 - 6) - linkages in 6,6-kestotetraose and (1 & 6)-kestotetraose at rates five times faster than the ẞ - (2 - 1) -linkages in 1,1-kestotetraose and (1 & 6)-kestotetraose. Fructose up to 50 mM did not affect 6-FEH activity; conversely, sucrose substantially inhibited the enzyme activity. Other disaccharides did not affect 6-FEH. It is suggested that sucrose might modulate 6-FEH activity in vivo."
Language:English
References:49
Note:Figures
Tables
ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Marx, S. P., J. Nösberger, and S. P. Marx. 1997. Hydrolysis of fructan in grasses: a ẞ - (2 - 6) - linkage specific fructan - ẞ - fructosidase from stubble of Lolium perenne. New Phytol. 135(2):p. 279-290.
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Web URL(s):
http://www.blackwell-synergy.com/doi/pdf/10.1046/j.1469-8137.1997.00642.x
    Last checked: 02/15/2006
    Requires: PDF Reader
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