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- W2348055488 abstract "Electrophoresis pure sucrase was obtained from Aspergillius niger TH-2 by a combination of ion exchange chromatography on DEAE-Sepharose column and Superdex-200 gel-filtration.The specific activity of the purified sucrase was 135.90 U/mg,the purification fold was 20.3,and 37.7% of the sucrase activity was reserved.This enzyme had a relative molecular weight of 1.29×105 and had two subunits.The optimum pH and temperature for this enzyme were 4.4 and 65 ℃,respectively.Its Michaelis-Menten Kinetics(Km) was 23.1 mmol/L.It was strongly inhibited by Ag+,and activated by Zn2+,Cu2+ and Mn2+." @default.
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- W2348055488 date "2011-01-01" @default.
- W2348055488 modified "2023-09-28" @default.
- W2348055488 title "Purification and Some Properties of Sucrase from Aspergillius niger TH-2" @default.
- W2348055488 hasPublicationYear "2011" @default.
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