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Properties of the deglycosylatedβ-fructofuranosidaseP-2 fromAureobasidium sp. ATCC 20524

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Journal of Industrial Microbiology

Summary

The carbohydrate moiety of β-fructofuranosidaseP-2 fromAureobasidium sp. ATCC 20524 was largely removed by exposure of the enzyme to endo-β-N-acetylglucosaminidase F; the total carbohydrate content of the enzyme was decreased from 53% (w/w) to 15% (w/w). The stability of the deglycosylated enzyme at pH 4 to 7 and 40 to 50°C was decreased and theK m value for sucrose was increased from 0.65 to 1.43 M. The deglycosylated enzyme was more sensitive to proteases such as pronase E and subtilisin than the native enzyme. It is concluded that the carbohydrate moiety of β-fructofuranosidaseP-2 contributes to the stability of the enzyme as well as its affinity for sucrose.

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Hayashi, S., Shimokawa, Y., Tubouchi, M. et al. Properties of the deglycosylatedβ-fructofuranosidaseP-2 fromAureobasidium sp. ATCC 20524. Journal of Industrial Microbiology 10, 191–194 (1992). https://doi.org/10.1007/BF01569765

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  • DOI: https://doi.org/10.1007/BF01569765

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