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Original scientific paper

https://doi.org/10.17113/ftb.53.02.15.3902

Purification and Characterization of an Endoinulinase from Xanthomonas campestris pv. phaseoli KM 24 Mutant

Kameshnee Naidoo ; Faculty of Applied Sciences, Durban University of Technology, Durban, Republic of South Africa
Ajit Kumar ; Faculty of Applied Sciences, Durban University of Technology, Durban, Republic of South Africa
Vikas Sharma ; Faculty of Applied Sciences, Durban University of Technology, Durban, Republic of South Africa
Kugen Permaul ; Faculty of Applied Sciences, Durban University of Technology, Durban, Republic of South Africa
Suren Singh ; Faculty of Applied Sciences, Durban University of Technology, Durban, Republic of South Africa


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Abstract

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 activity 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 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 apparent Km and vmax values of the inulinase when using inulin as a substrate 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 syrups.

Keywords

Xanthomonas campestris pv. phaseoli KM 24 mutant; inulinases; endoinulinases; exoinulinases; fructooligosaccharides; inulin

Hrčak ID:

140220

URI

https://hrcak.srce.hr/140220

Publication date:

23.6.2015.

Article data in other languages: croatian

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