Purification and Characterization of an Endoinulinase from Xanthomonas campestris pv. phaseoli KM 24 Mutant
| Autor: | Kameshnee Naidoo, Ajit Kumar, Vikas Sharma, Kugen Permaul, Suren Singh |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: | |
| Zdroj: | Food Technology and Biotechnology, Vol 53, Iss 2, Pp 146-153 (2015) |
| Druh dokumentu: | article |
| ISSN: | 1330-9862 1334-2606 |
| DOI: | 10.17113/ftb.53.02.15.3902 |
| 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: | Directory of Open Access Journals |
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