Effect of microenvironment of oxirane groups on the immobilization of penicillin G acylase
โ Scribed by R. V. Bahulekar; S. Ponrathnam; N. R. Ayyangar; K. K. Kumar; J. G. Shewale
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 427 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0021-8995
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The stabilisation of Escherichia coli penicillin G acylase (PGA) by dextran polymers (of molecular weight 11.5, 37.7 and 71 kDa) was studied. The inactivation of both the native and dextrancontaining enzyme preparations obeyed ยฎrst-order kinetics at the temperature and pH values studied. The optimal
The possibility of using the multicompartment immobilized enzyme reactor (MIER) in presence of a charged substrate is here explored. Penicillin G acylase is used to convert penicillin G (a free acid, with a pK of 2.6) into two charged products: phenyl acetic acid (PAA, with a pK of 4.2) and 6-aminop