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Titolo:
Cold-active lipolytic activity of psychrotrophic Acinetobacter sp strain no. 6
Autore:
Suzuki, T; Nakayama, T; Kurihara, T; Nishino, T; Esaki, N;
Indirizzi:
Kyoto Univ, Lab Microbial Biochem, Chem Res Inst, Kyoto 6110011, Japan Kyoto Univ Kyoto Japan 6110011 chem, Chem Res Inst, Kyoto 6110011, Japan Tohoku Univ, Dept Biomol Engn, Grad Sch Engn, Sendai, Miyagi 9808579, Japan Tohoku Univ Sendai Miyagi Japan 9808579 gn, Sendai, Miyagi 9808579, Japan
Titolo Testata:
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
fascicolo: 2, volume: 92, anno: 2001,
pagine: 144 - 148
SICI:
1389-1723(200108)92:2<144:CLAOPA>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENZYME-PURIFICATION; ADAPTED ENZYMES; GENE CLONING; BACTERIA; BIOTECHNOLOGY; LIPASE; ASSAY; FATS;
Keywords:
bioremediation; bioaugumentation; lipase; esterase; lipolytic enzyme; Acinetobacter;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Esaki, N Kyoto Univ, Lab Microbial Biochem, Chem Res Inst, Kyoto 6110011, Japan Kyoto Univ Kyoto Japan 6110011 m Res Inst, Kyoto 6110011, Japan
Citazione:
T. Suzuki et al., "Cold-active lipolytic activity of psychrotrophic Acinetobacter sp strain no. 6", J BIOSCI BI, 92(2), 2001, pp. 144-148

Abstract

A lipolytic bacterium, strain no. 6, was isolated from Siberian tundra soil. It was a gram-negative coccoid rod capable of growing at 4 degreesC but not at 37 degreesC and was identified as a psychrotrophic strain of the genus Acinetobacter. Strain no. 6 extracellularly produced a lipolytic enzyme that efficiently hydrolyzed triglycerides such as soybean oil during bacterial growth even at 4 degreesC; it degraded 60% of added soybean oil (initial concentration, 1% w/v) after cultivation in LB medium at 4 degreesC for 7d. Thus, the bacterium is potentially applicable to in-situ bioremediationor bioaugumentation of fat-contaminated cold environments. We partially purified the lipolytic enzyme from the culture filtrate by acetone fractionation and characterized it. The enzyme preparation contained a single speciesof cold-active lipase with significant activity at 4 degreesC, which was 57% of the activity at the optimum temperature (20 degreesC). The enzyme showed a broad specificity toward the acyl group (C-8-C-16) of substrate ethylesters.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 19:10:44