Please use this identifier to cite or link to this item: http://hdl.handle.net/10321/2962
Title: Purification and characterization of an Endoinulinase from Xanthomonas campestris pv. phaseoli KM 24 Mutant
Authors: Naidoo, Kameshnee 
Kumar, Ajit 
Sharma, Vikas 
Permaul, Kugen 
Singh, Suren 
Keywords: Xanthomonas campestris pv. phaseoli KM 24 mutant;Inulinases;Endoinulinases;Exoinulinases;Fructooligosaccharides;Inulin
Issue Date: 2015
Publisher: University of Zagreb
Source: 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.
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 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.
URI: http://hdl.handle.net/10321/2962
ISSN: 1330-9862
Appears in Collections:Research Publications (Applied Sciences)

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