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RECONSTITUTION OF DIFFERENT SIGNAL PEPTIDES FOR ENHANCED THERMOSTABLE ALPHA AMYLASE SECRETION IN Bacillus subtilis
| Content Provider | Semantic Scholar |
|---|---|
| Author | Thi, Nguyen Thoa, Nguyễn Thị Kim |
| Copyright Year | 2018 |
| Abstract | Three signal peptides of alpha amylase genes of three isolated strains that were Bacillus licheniformis DA23, Bacillus subtilis D5-2, Bacillus cereus CN1-5 were successfully sequenced. Three predicted “Sec – type” signal peptides have a length varying from 27 (CN1-5) to 33 residues (D5-2). The secretion of alpha amylase of the recombination B. subtilis 168MPgrac strain (pHV33–P grac Amy3BT2) with 71.4U/ml was larger than that of 168MPamy with 53.2U/ml. Base on analyzed rerults of PAGE and zymogram about molecular weight, alpha amylases in both strains were the same size, nearly 58kDa. The extracellular amylase activity of signal peptide S subtilisD5.2 in 168M was highest with 76.4±4.3 U/ml in four signal peptide targets. |
| Starting Page | 7 |
| Ending Page | 7 |
| Page Count | 1 |
| File Format | PDF HTM / HTML |
| DOI | 10.15625/2525-2518/56/1/9698 |
| Alternate Webpage(s) | http://vjs.ac.vn/index.php/jst/article/viewFile/9698/9049 |
| Alternate Webpage(s) | https://doi.org/10.15625/2525-2518%2F56%2F1%2F9698 |
| Volume Number | 56 |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |