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- W805295802 abstract "An extracellular inulinase from Penicillium sp. which isolated from soil sample was purified to a single protein th-rough ammonium sulfate fractionation, DEAE-Sephacel ion exchange chromatography and Toyopearl HW 65 F gel filtration. The temperature and pH for the enzyme reaction were around 6 and 4.0, respectively. The enzyme was stable at 3-5 and in the pH range of 4 to 5. , and EDTA inhibited the enzyme activity strongly. By contrast, and activated the enzyme activity. The molecular weight of the purified enzyme was esti-mated to be 77,000 dalton by SDS-polyacrylamide gel electrophoresis. The Km values of the enzyme for inulin were calculated to be M. TLC analysis suggested that purified enzyme is exo-type inulinase. The NH2-terminal amino acid sequences of the purified enzyme was determined to be -X-Glu-Ser-Tyr-Thr-Glu-Lys/Leu-Tyr-Arg-Pro." @default.
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- W805295802 date "1998-01-01" @default.
- W805295802 modified "2023-09-27" @default.
- W805295802 title "Purification and Characterization of Inulinase from Penicillium sp." @default.
- W805295802 hasPublicationYear "1998" @default.
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