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Extracellular secretion in Bacillus subtilis of a cytoplasmic thermostable β-galactosidase from Geobacillus stearothermophilus.
- Source :
-
Journal of Dairy Science . Jul2010, Vol. 93 Issue 7, p2838-2845. 8p. 1 Black and White Photograph, 2 Charts, 2 Graphs. - Publication Year :
- 2010
-
Abstract
- β-Galactosidase catalyzes the hydrolysis of β-galactosides into monosaccharides and is widely used in dairy processing. This study reports the extracellular secretion of a cytoplasmic thermostable β-galactosidase from Geobacillus stearothermophilus IAM11001 in Bacillus subtilis. This enzyme has potential applications in the dairy industry. It was not secreted in B. subtilis by mediation of 3 general secretory signal peptides, but was secreted extracellularly when it was fused to a twin-arginine signal peptide of B. subtilis phosphodiesterase. Defined and rich culture media were used for recombinant enzyme production, and the extracellular target enzymatic activity reached about 44% of the total enzymatic activity synthesized at 18h of cultivation in Luria-Bertani medium. As a control of secretion, when the signal peptide coding sequence was absent from the N terminus of the target gene bgaB, the extracellular target enzymatic activity obtained under the same condition of cultivation accounted for less than 7% of the total enzymatic activity synthesized. Results also showed that coexpression of the B. subtilis proteins TatAd and TatCd was indispensable for the secretion of the target enzyme. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00220302
- Volume :
- 93
- Issue :
- 7
- Database :
- Academic Search Index
- Journal :
- Journal of Dairy Science
- Publication Type :
- Academic Journal
- Accession number :
- 52045230
- Full Text :
- https://doi.org/10.3168/jds.2009-2864