Puriﬁcation and characterization of an Endoinulinase from Xanthomonas campestris pv. phaseoli KM 24 Mutant
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An 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.
Naidoo, 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.