Naidoo, KameshneeKumar, AjitSharma, VikasPermaul, KugenSingh, Suren2018-05-152018-05-152015Naidoo, K. et al. 2015. Purification and characterization of an Endoinulinase from Xanthomonas campestris pv. phaseoli KM 24 Mutant. Food Technology and Biotechnology. 53(2): 146–153.1330-9862http://hdl.handle.net/10321/2962An extracellular endoinulinase from Xanthomonas campestris pv. phaseoli KM 24 mutant was purifi ed to homogeneity by gel fi ltration chromatography and showed a specifi c activ-ity of 119 U/mg. The optimum pH and temperature of the purifi ed enzyme were found to be 6.0 and 50 °C, respectively. The enzyme was stable up to 60 °C, retaining 60 % of residu-al activity for 30 min, but inactivated rapidly above 60 °C. The enzyme was found to be stable at pH=6–9 when it retained 100 % of its residual activity. The Lineweaver-Burk plot showed that the apparent Km and vmax values of the inulinase when using inulin as a sub-strate were 1.15 mg/mL and 0.15 μM/min, respectively, whereas the kcat value was found to be 0.145 min–1. The calculated catalytic effi ciency of the enzyme was found to be 0.126 (mg·min)/mL. The purifi ed inulinase can be used in the production of high fructose syr-ups.8 penXanthomonas campestris pv. phaseoli KM 24 mutantInulinasesEndoinulinasesExoinulinasesFructooligosaccharidesInulinArticle10.17113/ft b.53.02.15.3902