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Titolo:
Formation of lipolytic enzymes by Brevibacterium linens
Autore:
Adamitsch, BF; Hampel, WA;
Indirizzi:
Vienna Univ Technol, Inst Biochem Technol & Microbiol, A-1060 Vienna, Austria Vienna Univ Technol Vienna Austria A-1060 robiol, A-1060 Vienna, Austria
Titolo Testata:
BIOTECHNOLOGY LETTERS
fascicolo: 20, volume: 22, anno: 2000,
pagine: 1643 - 1646
SICI:
0141-5492(200010)22:20<1643:FOLEBB>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
PURIFICATION; PROTEINASE; LIPASES;
Keywords:
Brevibacterium linens; lipase-formation; lipase-location;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
14
Recensione:
Indirizzi per estratti:
Indirizzo: Adamitsch, BF Vienna Univ Technol, Inst Biochem Technol & Microbiol, Getreidemarkt 9-172, A-1060 Vienna, Austria Vienna Univ Technol Getreidemarkt 9-172 Vienna Austria A-1060
Citazione:
B.F. Adamitsch e W.A. Hampel, "Formation of lipolytic enzymes by Brevibacterium linens", BIOTECH LET, 22(20), 2000, pp. 1643-1646

Abstract

When Brevibacterium linens ATCC 9172 was grown in shake flasks, it produced a cell-associated lipase with a specific activity of 152 to 188 U g(-1) cells depending on the composition of the growth medium. There was no growthin media containing tributyrine as the sole carbon source. The cell-associated lipase had maximum activity at pH 8.0 and 37 degreesC and was stronglyinhibited by 3,4-dichloroisocoumarin, an inhibitor specific for serine esterases. Cell-associated activity was released from the cells by treatment with lysozyme. The kinetics of lipase formation was closely related to the amount of biomass formed during growth.

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Documento generato il 15/07/20 alle ore 08:38:15