Purification and properties of an endo-inulinase from an Arthrobacter sp.

Authors
Kang, SI Chang, YJ Oh, SJ Kim, SI
Citation
Si. Kang et al., Purification and properties of an endo-inulinase from an Arthrobacter sp., BIOTECH LET, 20(10), 1998, pp. 983-986
Citations number
11
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
BIOTECHNOLOGY LETTERS
ISSN journal
01415492 → ACNP
Volume
20
Issue
10
Year of publication
1998
Pages
983 - 986
Database
ISI
SICI code
0141-5492(199810)20:10<983:PAPOAE>2.0.ZU;2-K
Abstract
Extracellular endo-inulinase of Arthrobacter sp. S37 was purified 63-fold, giving a single band on PAGE with activity staining. The M-r was estimated as 75 kDa by SDS-PAGE. The first 31 amino acids of the N-terminal sequence was determined. The endo-inulinase hydrolyzed inulin mainly into inulo-trio se (F3), inulo-tetraose (F4) and inulo-pentaose (F5) optimally at pH 7.5 an d 50 degrees C.