Work

Effect of deglycosylation on the properties of β-fructofuranosidaseP-1 fromAureobasidium sp. ATCC 20524

Year: 1992

Type: article

Abstract: Most of the carbohydrate moiety of β-fructofuranosidaseP-1 fromAureobasidium sp. ATCC 20524 was removed by endo-β-N-acetylglucosaminidase F. A subunit of 94000 Da was observed in SDS-PAGE after deglycosylation. TheKm value for sucrose was not changed by deglycosylation but the stability at pH 4–5 and 50°C was decreased. The deglycosylated enzyme was more sensitive to proteases such as pronase E and subtilisin than the native enzyme. It is considered that the carbohydrate moiety of β-fructofuranosidaseP-1 contributes to the stability of the enzyme but is not essential in its catalytic function.

Source: Journal of Industrial Microbiology & Biotechnology

DOI: 10.1007/bf01569632

Authors: Sachio Hayashi, Masaharu Nonoguchi, Yoshihiko Shimokawa, Yoshiyuki Takasaki, Kiyohisa Imada

Institution: University of Miyazaki

Language: English

Topic: Enzyme Production and Characterization

Subfield: Biotechnology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2017065285

FWCI: 0.749

Cites: 10

Cited by: 7

Related to: 10