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Titolo:
Screening and characterization of trehalose-oleate hydrolyzing lipase
Autore:
Ishimoto, R; Sugimoto, M; Kawai, F;
Indirizzi:
Okayama Univ, Bioresources Res Inst, Kurashiki, Okayama 7100046, Japan Okayama Univ Kurashiki Okayama Japan 7100046 hiki, Okayama 7100046, Japan
Titolo Testata:
FEMS MICROBIOLOGY LETTERS
fascicolo: 2, volume: 195, anno: 2001,
pagine: 231 - 235
SICI:
0378-1097(20010220)195:2<231:SACOTH>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOMONAS-CEPACIA; PURIFICATION;
Keywords:
trehalose-oleate; lipase; Burkholderia species;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
14
Recensione:
Indirizzi per estratti:
Indirizzo: Ishimoto, R Okayama Univ, Bioresources Res Inst, 2-20-1 Chuo, Kurashiki, Okayama 7100046, Japan Okayama Univ 2-20-1 Chuo Kurashiki Okayama Japan 7100046 Japan
Citazione:
R. Ishimoto et al., "Screening and characterization of trehalose-oleate hydrolyzing lipase", FEMS MICROB, 195(2), 2001, pp. 231-235

Abstract

Various soil samples were collected to screen the presence of microorganisms which have ability to degrade TOE. One strain (AKU-883) with good TOE degrading activity was isolated and identified as Burkholderia cepacia and the extracellular enzyme was purified to homogeneity. The purification was achieved by ultrafiltration. Super Q anion-exchange chromatography and Superdex 200HR gel-filtration in the presence of Triton X. The enzyme was purified to 85-fold. and specific activity of 4.910 kU mg protein(-1). The peak preparation on gel filtration showed a single band of 34 kDa on SDS-PAGE and native PAGE which indicate the monomeric nature of the enzyme. The pr of the enzyme was 6.3. The enzyme showed the maximum activity at pH 9 and 65 degreesC. and was stable in the range of pH 5-10 and up to 60 degreesC. Almostall the activity (92%) was kept after incubation for more than 1 week at 50 degreesC (pH 7.3). High activities remained even in water-miscible solvents such as ethanol, dimethyl formamide, diisopropyl ether, and dioxane, TheN-terminal 16 amino acid residues were determined as A-N-G-Y-A-A-T-R-Y-P-I-I-L-V-G-G. which showed a consensus sequence for lipases from Burkholderiaspecies. Thus the enzyme was concluded to be a kind of lipase. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/10/20 alle ore 13:30:35