title: Purification and Characterization of an Endoinulinase fromXanthomonas campestrispv.phaseoliKM 24 Mutant.
abstract: An extracellular endoinulinase fromXanthomonas campestrispv.phaseoliKM 24 mutant was purified to homogeneity by gel filtration chromatography and showed a specific activity of 119 U/mg. The optimum pH and temperature of the purified enzyme were found to be 6.0 and 50 °C, respectively. The enzyme was stable up to 60 °C, retaining 60% of residual 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 apparentKmandvmaxvalues of the inulinase when using inulin as a substrate were 1.15 mg/mL and 0.15 µM/min, respectively, whereas thekcatvalue was found to be 0.145 min-1. The calculated catalytic efficiency of the enzyme was found to be 0.126 (mg·min)/mL. The purified inulinase can be used in the production of high fructose syrups.
authors.forename: Kameshnee
authors.initials: K
authors.lastname: Naidoo
authors.forename: Ajit
authors.initials: A
authors.lastname: Kumar
authors.affiliation: Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, P.O. Box 1339, Durban 4001, Republic of South Africa.
authors.forename: Vikas
authors.initials: V
authors.lastname: Sharma
authors.affiliation: Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, P.O. Box 1339, Durban 4001, Republic of South Africa.
authors.forename: Kugen
authors.initials: K
authors.lastname: Permaul
authors.affiliation: Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, P.O. Box 1339, Durban 4001, Republic of South Africa.
authors.forename: Suren
authors.initials: S
authors.lastname: Singh
keywords: Xanthomonas campestris pv. phaseoli KM 24 mutant; endoinulinases; exoinulinases; fructooligosaccharides; inulin; inulinases