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Title 

Purification and properties of inulaseII from arthrobacter ureafaciens KCTC 3387

 

Arthrobacter ureafaciens KCTC 3387이 생산하는 inulase II의 정제 및 특성

Authors 

Jae Chan LeeKi Young LeeKi Bang SongYong Bok Lee

Publisher 

Korean Journal of Applied Microbiology and Biotechnology

Issue Date 

1999

Citation 

Korean Journal of Applied Microbiology & Biotechnology, vol. 27, no. 6, pp. 471-476

Keywords 

Arthrobacter ureafaciens KCTC 3387DFAIIIInulaseIIInulinArthrobacterenzyme purificationArthrobacter ureafaciens

Abstract 

Inulin fructotransferase(depolymerizing)(EC 2.4.1.93)(inulaseII) which converts inulin into di-D-fructofuranose-1,2':2,3'-dianhydride (DFAIII) was purified from Arthrobacter ureafaciens KCTC 3387 using column chromatography on DEAE-Toyopearl 650 M and gel filtration on Sephadex G-200. The enzyme was purified 7-fold with a yield of 11% from a culture supernatant. The purified enzyme gave a single band on polyacrylamide gel electrophoresis, and the molecular weight of the enzyme was estimated to be 45,000 by SDS- polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme reaction were pH 6.5-7.0 and 55°C, respectively. The enzyme was stable within a pH range of 5.0 to 10.6 and up to 60°C. The K(m) of this enzyme for DFAIII production was 11.9 mM. The enzyme was inactivated by Hg2+ and after exhaustive digestion of inulin by this enzyme, 1-kestose and nystose were produced in addition to DFAIII.

ISSN 

0257-2389

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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