Purification and Characterization of an Endoinulinase from Xanthomonas campestris pv. phaseoli KM 24 Mutant
| Autor: | Ajit Kumar, Vikas Sharma, Suren Singh, Kugen Permaul, Kameshnee Naidoo |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
fructooligosaccharides
lcsh:Biotechnology General Chemical Engineering Size-exclusion chromatography Inulin Xanthomonas campestris pv. phaseoli KM 24 mutant Industrial and Manufacturing Engineering Microbiology chemistry.chemical_compound lcsh:TP248.13-248.65 endoinulinases Enzyme kinetics Inulinase chemistry.chemical_classification Chromatography inulin lcsh:TP368-456 biology biology.organism_classification exoinulinases Enzyme assay Xanthomonas campestris lcsh:Food processing and manufacture Enzyme chemistry biology.protein Specific activity inulinases Food Science Biotechnology |
| Zdroj: | Food Technology and Biotechnology, Vol 53, Iss 2, Pp 146-153 (2015) |
| ISSN: | 1334-2606 1330-9862 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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