Abstract
A mixed-gel of κ-carrageenan and gelatin was used in l-phenylalanine production. The mixed-gel, containing 87.5% κ-carrageenan and 12.5% gelatin [the total gel concentration was 4 wt%], showed the best performance and was selected for further study with Escherichia coli EP8-10. The optimum pH and temperature were 8.5 and 37 °C, respectively. The effects of trehalose and Mg2+ were studied in the mixed-gel immobilization. Their optimum concentrations were 5 × 10-2 and 2 × 10-3 mol/L, respectively. Under the optimal conditions, 98.3% of the phenylpyruvic acid (PPA) was converted to l-phenylalanine. The activity recovery of the transaminase enzyme in the mixed-gel immobilization was higher than that in single κ-carrageenan immobilization, which was 93.6%. The total PPA conversion rate was over 80% in all 15 batches, suggesting great sustainability in the mixed-gel immobilization. The maximum reaction rate (rmax) was calculated to be 4.75 × 10-2 mol/(L g h). Crown
Original language | English |
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Pages (from-to) | 142-145 |
Number of pages | 4 |
Journal | Process Biochemistry |
Volume | 44 |
Issue number | 2 |
DOIs | |
State | Published - Feb 2009 |
Keywords
- Bioconversion
- Gelatin
- Mixed-gel immobilization
- Transaminase
- l-Phenylalanine
- κ-Carrageenan