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• W2548871507 abstract "The purification and characterization of the extracellular polygalacturonase from Zygoascus hellenicus V25 submerged culture using orange peel waste were investigated. This polygalacturonase, with a molecular weight of 75.28 kDa, was purified to 16.89 purification fold with a recovery of 18.46% and specific activity of 2469.77 U/mg protein by ammonium sulfate precipitation, DEAE cellulose chromatography, and Sephadex G-100 gel filtration. The enzyme exhibited maximum activity at 60°C and pH 5.0 and was stable over a wide range of pH levels (3.0-11.0). Moreover, enzyme activity was enhanced by Cu2+ and cysteine, whereas it was strongly inhibited by Hg2+. The extent of enzymatic hydrolysis was negatively correlated with the degree of pectin esterification. Km and Vmax values of the polygalacturonase were 5.44 mg/mL and 61.73 μmol/(min·mg), respectively. The polygalacturonase was applied in the juice clarification of four fruits, and results showed that the percentage transmittance at 660 nm increased by 3.51, 4.36, 8.04, and 12.2%." @default.
• W2548871507 created "2016-11-11" @default.
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• W2548871507 date "2016-10-01" @default.
• W2548871507 modified "2023-10-16" @default.
• W2548871507 title "Purification and characterization of exo-polygalacturonase from Zygoascus hellenicus V25 and its potential application in fruit juice clarification" @default.
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• W2548871507 doi "https://doi.org/10.1007/s10068-016-0215-3" @default.
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