Isolation, Purification, and Properties of Naringinase Produced from Aspergillus niger FFCC 848 by Liquid Fermentation
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Abstract:
The isolation, purification, and enzymatic properties of naringinase produced by liquid fermentation with Aspergillus niger FFCC 848 were investigated. The fermentation broth produced from liquid fermentation by A. niger FFCC 848 was purified by ammonium sulfate fractional precipitation, dialysis, and DEAE-Sepharose FF anion exchange chromatography to yield highly purified naringinase. Only one clear band was observed upon sodium dodecyl sulfate polyacrylamide gel electrophoresis, with a molecular weight of 65.10 ku. The final, purified naringinase showed 13.82-fold purification, with an enzyme activity recovery of 13.30% and specific activity of 6932.54 U/mg, and the enzyme could effectively hydrolyze naringin. Furthermore, the activity of naringinase was stable at 20–50?C and pH 3.0–6.0; optimum activity was observed at 50?C and pH 4.5. In a specific concentration range, the enzyme activity was enhanced by K+, Ca2+, and Na +, but was strongly inhibited by Fe3+, SDS, and EDTA-Na2. This study provides a basis for understanding the purification of naringinase and for further studies of the related mechanism underlying the bioconversion of bioactive natural products with naringinase.
