Abstract
Penicillium decumbens PTCC 5248 produced naringinase when grown in a medium contained naringin as a source of carbon. Rhamnose also induced production of naringinase. Prunin disappeared as the time of enzymatic reaction increased. On fractionation with isopropanol 24-fold purification was achieved. Optimum pH and temperature for naringinase activity were determined to be 4.5 and 55 °C respectively. The Km value of the enzyme with respect to naringin was found to be 1.7 mM. Citric acid, glucose, Ca2+, Mg2+, Zn2+ all inhibited naringinase activity.
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Norouzian, D., Hosseinzadeh, A., Inanlou, D.N. et al. Production and partial purification of naringinase by Penicillium decumbens PTCC 5248. World Journal of Microbiology and Biotechnology 16, 471–473 (2000). https://doi.org/10.1023/A:1008962131271
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DOI: https://doi.org/10.1023/A:1008962131271