Penicillin Acylase-Catalyzed Solid-State Ampicillin Synthesis

✍ Scribed by M. I. Youshko; V. K. Švedas

• Publisher: John Wiley and Sons
• Year: 2002
• Tongue: English
• Weight: 71 KB
• Volume: 344
• Category: Article
• ISSN: 1615-4150
• DOI: 10.1002/1615-4169(200209)344:8<894::aid-adsc894>3.0.co;2-q

✦ Synopsis

The ability of immobilized penicillin acylase from E. coli to retain a remarkable catalytic activity in solid-state systems has been demonstrated. Stabilization of immobilized penicillin acylase by inorganic salt hydrates allowed us to exploit nearly the whole catalytic activity of the enzyme at a very low water content. Using this technique, enzymatic synthesis of ampicillin in solid-state systems was performed with high yields (up to 70% starting from equimolar mixture of reagents) and rates comparable to the corresponding values in homogeneous solutions and heterogeneous systems, ™aqueous solution-precipi-tate∫. Peculiarities of the enzymatic solid-state acyl transfer process, such as absence of the clear-cut maximum on the ampicillin accumulation curves and dependence of the synthetic efficiency on the enzyme loading, have been observed. The space-time yield of solid-state enzymatic ampicillin synthesis was shown to be up to ten times higher compared to the homogeneous solutions and heterogeneous ™aqueous solution-precipitate∫ systems.