Izvorni znanstveni članak
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
Sažetak
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.
Ključne riječi
Xanthomonas campestris pv. phaseoli KM 24 mutant; inulinases; endoinulinases; exoinulinases; fructooligosaccharides; inulin
Hrčak ID:
140220
URI
Datum izdavanja:
23.6.2015.
Posjeta: 1.349 *