ISSN:
1476-5535
Keywords:
β-Fructofuranosidase
;
Deglycosylation
;
Aureobasidium
;
Enzymatic stability
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01569765
