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• W2016972556 abstract "A psychrotolerant yeast Guehomyces pullulans 17-1 isolated from sea sediment in Antarctica could produce high level (17.2 U/ml) of both extracellular and cell-bound β-galactosidase. The extracellular β-galactosidase in the supernatant of the cell culture of the psychrotolerant yeast G. pullulans 17-1 was purified to homogeneity with a 2.4-fold increase in specific activity as compared to the supernatant by concentration, gel filtration chromatography (Sephadex G-200) and cation-exchange chromatography (CM-Sepharose Fast Flow cation-exchange). The molecular mass of the purified extracellular β-galactosidase was estimated to be 335 kDa. The optimal temperature and pH of the purified β-galactosidase were 50 °C and 4.0, respectively. Km and Vmax values of the purified β-galactosidase for o-nitrophenyl-β-d-galactopyranoside were 3.3 mM and 9.2 μmol/min. Lactose can be converted into glucose and galactose and a large amount of reducing sugar can be released from milk under catalysis of the purified β-galactosidase. The matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectroscopy identified a peptide ALEEYKK which is the conserved motif of the β-galactosidases from other yeasts. The results show that the enzyme may have potential applications in food industry." @default.
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• W2016972556 date "2010-06-01" @default.
• W2016972556 modified "2023-10-09" @default.
• W2016972556 title "Purification and characterization of extracellular β-galactosidase from the psychrotolerant yeast Guehomyces pullulans 17-1 isolated from sea sediment in Antarctica" @default.
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• W2016972556 doi "https://doi.org/10.1016/j.procbio.2010.02.025" @default.
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