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Genistein and daidzein are isoflavones with well-recognized biological activities. Their glycosidic forms (genistin and daidzin, respectively) are abundant in some plants. In this study, production of β-glucosidase from Penicillium janthinellum NCIM 1171 and its use in the obtaining genistein and daidzein are described. In a response surface methodology (RSM) optimized medium, levels of β-glucosidase under submerged and solid state fermentation conditions were found to be 10.2 ± 0.75 IU/mL and 121 ± 9.3 IU/g, respectively. The supernatants resulting from submerged fermentation were subjected to ion exchange and gel filtration chromatography and the enzyme was purified in a 44.4 fold manner with final recovery of 39.75 %. The β-glucosidase was deduced to be a monomeric protein with a molecular mass of 97.18 kDa. The purified protein showed 46 % sequence coverage matching with β-glucosidase derived from Penicillium sp. ABP88968. The purified enzyme was effective in producing genistein and daidzein from soybean (Glycine max) flour extract with a yield of 92.3 and 95 %, respectively. To the best of our knowledge, this is the first report on the use of a wild type strain of P. janthinellum for the production of genistein and daidzein with high productivity and purity. |
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