Secretion of a heterologous cytoplasmic b-galactosidase in Bacillus subtilis
首发时间:2008-12-29
Abstract:A cytoplasmic b-galactosidase (BgaB) from Geobacillus stearothermophilus IAM11001, which can not be secreted in Bacillus subtilis by mediation of two general secretory signal peptides, was secreted in Bacillus subtilis when it was fused to a twin-arginine signal peptide. The extracellular BgaB enzymatic activity accounted for about 39% of the total enzymatic activity at 18 h of cultivation in Luria-Bertani medium. As a control of secretion, the extracellular BgaB enzymatic activity obtained at the same time of cultivation accounted for less than 3% of the total enzymatic activity when the signal peptide coding sequence was absent from the N-terminus of the target gene bgaB.
keywords: Bacillus subtilis protein secretion b-galactosidase twin-arginine translocation signal peptide enzymatic activity
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Secretion of a heterologous cytoplasmic b-galactosidase in Bacillus subtilis
摘要:A cytoplasmic b-galactosidase (BgaB) from Geobacillus stearothermophilus IAM11001, which can not be secreted in Bacillus subtilis by mediation of two general secretory signal peptides, was secreted in Bacillus subtilis when it was fused to a twin-arginine signal peptide. The extracellular BgaB enzymatic activity accounted for about 39% of the total enzymatic activity at 18 h of cultivation in Luria-Bertani medium. As a control of secretion, the extracellular BgaB enzymatic activity obtained at the same time of cultivation accounted for less than 3% of the total enzymatic activity when the signal peptide coding sequence was absent from the N-terminus of the target gene bgaB.
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Secretion of a heterologous cytoplasmic b-galactosidase in Bacillus subtilis
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