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Production, Purification, and Characterization of Polygalacturonase from Mucor circinelloides ITCC 6025

Author(s): Akhilesh Thakur | Roma Pahwa | Smarika Singh | Reena Gupta

Journal: Enzyme Research
ISSN 2090-0406

Volume: 2010;
Date: 2010;
Original page

Mucor circinelloides produced an extracellular polygalacturonase enzyme, the production of which was enhanced when various production parameters were optimized. Maximum polygalacturonase (PGase) activity was obtained in 48 h at 30∘C and pH 4.0 with pectin methyl ester (1% w/v) as carbon source and a combination of casein hydrolysate (0.1% w/v) and yeast extract (0.1% w/v) as nitrogen source. The enzyme was purified to homogeneity (13.3-fold) by Sephacryl S-100 gel-filtration chromatography. Its molecular weight was 66 kDa on SDS-PAGE. The enzyme was found to have Km and Vmax values of 2.2 mM and 4.81 IU/ml at 0.1% to 0.5% (w/v) concentration of the substrate. The addition of phenolic acids (0.05 mM), metal ions such as Mn+2, Co+2, Mg+2, Fe+3, Al+3, Hg+2, and Cu+2, and thiols had inhibitory effect on the enzyme. The enzyme showed maximum activity in the presence of polygalacturonic acid (0.1% w/v) at pH 5.5 and 42∘C.
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