Influence of mass transfer limitations on the enzymatic synthesis of β-lactam antibiotics catalyzed by penicillin G acylase immobilized on glioxil-agarose

被引:18
|
作者
Goncalves, L. R. B. [1 ]
Ferreira, A. L. O. [1 ]
Fernandez-Lafuente, R. [2 ]
Guisan, J. M. [2 ]
Giordano, R. C. [3 ]
Giordano, R. L. C. [3 ]
机构
[1] Univ Fed Ceara, Dept Engn Quim, BR-60455760 Fortaleza, Ceara, Brazil
[2] CSIC, Inst Catalisis & Petr Quim, Madrid, Spain
[3] Univ Fed Sao Carlos, Dept Engn Quim, BR-13565905 Sao Carlos, SP, Brazil
基金
巴西圣保罗研究基金会;
关键词
mass transfer effects; penicillin G acylase; amoxicillin; ampicillin; immobilized enzyme; beta-lactam antibiotics;
D O I
10.1007/s00449-007-0176-2
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Mass transfer effects were investigated for the synthesis of ampicillin and amoxicillin, at pH 6.5 and 25 degrees C, catalyzed by penicillin G acylase immobilized on agarose. The influence of external mass transfer was analysed using different stirring rates, ranging form 200 to 800 rpm. Above 400 rpm, the film resistance may be neglected. Intra-particle diffusion limitation was investigated using biocatalysts prepared with different enzyme loads and agarose with different mean pore diameters. When agarose with 6, 8 and 10% of crosslinking were used, for the same enzyme load, substrates and products concentration profiles presented no expressive differences, suggesting pore diameter is not important parameter. An increase on enzyme load showed that when more than 90 IU of enzyme activity were used per mL of support, the system was influenced by intra-particle mass transfer. A reactive-diffusive model was used to estimate effective diffusivities of substrates and products.
引用
收藏
页码:411 / 418
页数:8
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