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Characterization of Neutral Invertase from Fast Growing Pea (Pisum sativum L.) Seedlings after Gibberellic Acid (GA) Treatment
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  • Journal title : Journal of Life Science
  • Volume 25, Issue 9,  2015, pp.1021-1026
  • Publisher : Korean Society of Life Science
  • DOI : 10.5352/JLS.2015.25.9.1021
 Title & Authors
Characterization of Neutral Invertase from Fast Growing Pea (Pisum sativum L.) Seedlings after Gibberellic Acid (GA) Treatment
Kim, Donggiun;
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Invertase (β-D-fructosfuranosidase, EC catalyzes the hydrolysis of sucrose into D-glucose and D-fructose. Three biochemical subgroups of invertases have been investigated in plants: vacuolar (soluble acid), cytoplasmic (soluble alkaline), and cell wall-bound (insoluble acid) invertases. An isoform of neutral invertase was purified from pea seedlings (Pisum sativum L.) and treated with gibberellic acid (GA) by sequential procedures consisting of ammonium sulfate precipitation, ion-exchange chromatography, absorption chromatography, and reactive green-19 affinity chromatography. The results of the overall insoluble invertase purification were a 430-fold increase. The purified neutral invertase was not glycosylated and had an optimum pH between neutral and alkaline (pH 6.8-7.5). It was inhibited by Tris, as well as by heavy metals, such as Hg2+ and Cu2+. Typical Michaelis–Menten kinetics were observed when the activity of the purified invertase was measured, with sucrose concentrations up to 100 mM. The Km and Vmax values were 12.95 mM and 2.98 U/min, respectively. The molecular mass was around 20 kDa. The sucrose-cleaving enzyme activity of this enzyme is similar to that of sucrose synthase and fructosyltransferase, but its biochemical characteristics are different from those of sucrose synthase and fructosyltransferase. Based on this biochemical characterization and existing knowledge, neutral INV is an invertase isoform in plants.
β-D-fructosfuranosidase;characterization;Pisum sativum L.;neutral invertase;purification;
 Cited by
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