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- 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
- Abstract
An extracellular endoinulinase from Xanthomonas campestris pv. phaseoli KM 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 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 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.
- Subjects
XANTHOMONAS campestris; PHASEOLIN; INULASE; BACTERIAL mutation; BACTERIAL enzymes -- Inactivation; GEL permeation chromatography
- Publication
Food Technology & Biotechnology, 2015, Vol 53, Issue 2, p146
- ISSN
1330-9862
- Publication type
Article
- DOI
10.17113/ftb.53.02.15.3902