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Titolo:
Isolation of a protease-deficient mutant of Bacillus brevis and efficient secretion of a fungal protein disulfide isomerase by the mutant
Autore:
Kajino, T; Kato, K; Miyazaki, C; Asami, O; Hirai, M; Yamada, Y; Udaka, S;
Indirizzi:
Toyota Cent Res & Dev Labs Inc, Aichi 4801192, Japan Toyota Cent Res & DevLabs Inc Aichi Japan 4801192 Aichi 4801192, Japan Tokyo Univ Agr, Dept Fermentat Sci, Tokyo 156, Japan Tokyo Univ Agr Tokyo Japan 156 Agr, Dept Fermentat Sci, Tokyo 156, Japan
Titolo Testata:
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
fascicolo: 1, volume: 87, anno: 1999,
pagine: 37 - 42
SICI:
1389-1723(199901)87:1<37:IOAPMO>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; SODIUM DODECYL-SULFATE; HIGH-LEVEL SECRETION; POLYACRYLAMIDE GELS; ELECTROPHORETIC TRANSFER; ESCHERICHIA-COLI; ANTIBODY; NITROCELLULOSE; PURIFICATION; INHIBITOR;
Keywords:
Bacillus brevis; secretion; protease-deficient mutant; protein disulfide isomerase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Kajino, T Toyota Cent Res & Dev Labs Inc, Aichi 4801192, Japan Toyota CentRes & Dev Labs Inc Aichi Japan 4801192 1192, Japan
Citazione:
T. Kajino et al., "Isolation of a protease-deficient mutant of Bacillus brevis and efficient secretion of a fungal protein disulfide isomerase by the mutant", J BIOSCI BI, 87(1), 1999, pp. 37-42

Abstract

The efficient production of a thermostable protein disulfide isomerase (PDI) was successfully achieved using the newly isolated protease-deficient mutant, Bacillus brevis 31-OK. Extracellular protease (exoprotease) activity was about a quarter of that in the parent, and the mutant was deficient in at least one of the major exoproteases. The cDNA encoding the fungal PDI was inserted downstream of the signal peptide-encoding region in an expression-secretion vector for B. brevis. Efficient production of PDI was feasible using B. brevis 31-OK as a host and modified signal sequences composed of three leucine residues inserted in the hydrophobic region of the MWP (middlewall protein) signal sequence. The maximal secretion of PDI into the culture medium was 1.1 g/l, which is about twice that by the parent strain and fifty times greater than the amount of rat and murine PDIs produced by Escherichia coli. The enzymatic properties such as the specific activity and thermal stability of the recombinant PDI are similar to those of natural PDI derived from Humicola insolens mycelia. B. brevis 31-OK was able to maintainits exoprotease activity at a low level throughout the cultivation and is considered to be useful host for production of a protease-sensitive proteinand for increase of protein productivity due to stable accumulation.

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Documento generato il 26/11/20 alle ore 11:39:59