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- W2021025666 abstract "Purification of β-glucosidase from the seeds of Japanese cycad, and properties of the purified preparation are described. The enzyme activity was determined by colorimetry using ONPG as substrate. Crude preparation was obtained easily by adsorption on fibrous CMC pulp. It was further purified by chromatography on CMC powder, and a preparation which showed an activity of 135-folds of the original extract was obtained. Influences of pH, temperature, and substrate concentration upon the enzyme activity were examined. Michaelis constant of the enzyme for ONPG was 3.3×10–3M. Some evidences indicating existence of free aglycon of cycasin are described. Cycasin was hydrolysed with purified cycad β-glucosidase, and the freed sugar component and aglycon were analyzed by manometry or quantitative paper chromatography and by spectrophotometry or polarography, respectively. When the hydrolysis was stopped by ice-cooling or by acidification, the reaction mixture showed the characteristic absorption spectrum and polarogram similar to those of cycasin in spite of the liberation of glucose. However, if the reaction was stopped by heating, the spectrum and polarogram were not observed. This fact was considered to indicate that the free aglycon of cycasin formed in its enzymatic hydrolysis was decomposed by the heat treatment." @default.
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- W2021025666 date "1962-04-01" @default.
- W2021025666 modified "2023-10-16" @default.
- W2021025666 title "Biochemical Studies on Cycasin" @default.
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- W2021025666 doi "https://doi.org/10.1080/00021369.1962.10857964" @default.
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