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1. (Article ID: 9132)
 
Ojwach J, Kumar A, Mukaratirwa S, Mutanda T
Purification and biochemical characterization of an extracellular fructosyltransferase enzyme from Aspergillus niger sp. XOBP48: implication in fructooligosaccharide production
3 Biotech 10(10) (2020) ID 459
 

An extracellular fructosyltransferase (Ftase) enzyme with a molar mass of ≈70 kDa from a newly isolated indigenous coprophilous fungus Aspergillus niger sp. XOBP48 is purified to homogeneity and characterized in this study. The enzyme was purified to 4.66-fold with a total yield of 15.53% and specific activity of 1219.17 U/mg of protein after a three-step procedure involving (NH4)2SO4 fractionation, dialysis and anion exchange chromatography. Ftase showed optimum activity at pH 6.0 and temperature 50 °C. Ftase exhibited over 80% residual activity at pH range of 4.0-10.0 and ≈90% residual activity at temperature range of 40-60 °C for 6 h. Metal ion inhibitors Hg2+ and Ag+ significantly inhibited Ftase activity at 1 mmol concentration. Ftase showed Km, vmax and kcat values of 79.51 mmol, 45.04 µmol/min and 31.5 1/min, respectively, with a catalytic efficiency (kcat/Km) of 396 1/µmol/min for the substrate sucrose. HPLC-RI experiments identified the end products of fructosyltransferase activity as monomeric glucose, 1-kestose (GF2), and 1,1-kestotetraose (GF3). This study evaluates the feasibility of using this purified extracellular Ftase for the enzymatic synthesis of biofunctional fructooligosaccharides.

1-kestose, 1, fructooligosaccharides, Aspergillus niger, fructosyltransferase, zymography, 1-kestotetraose

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