Abstract
The methionine adenosyltransferase (MAT) gene is cloned from the genome of E. Coli-K12, and the recombinant E. Coli JM109(pBR322-MAT) strain which can highly express MAT is constructed. The whole cells of E. Coli JM109 (PBR322-MAT) are immobilized in Ca-alginate(CA) gel. The optimal mass concentration of CA is 20 g/L and the optimal cell loading by direct entrapment is 0.15 g of wet weight cells per mL gel. After 5 batches of reaction, the enzyme activity decreases to 91% of the initial. For the biosynthesis of S-adenosylmethionine by immobilized cell, the conversion rate based on the amount of ATP can be over 95 % under the optimal conditions.
| Original language | English |
|---|---|
| Pages (from-to) | 38-41+43 |
| Journal | Xiandai Huagong/Modern Chemical Industry |
| Volume | 29 |
| Issue number | 3 |
| State | Published - Mar 2009 |
Keywords
- Escherichia coli
- Immobilized cell
- Recombinant cell
- S-adenosylmethionine
- Whole-cell catalyst
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