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首页> 外文期刊>Applied Microbiology and Biotechnology >Enzymatic synthesis of cephalosporins. The immobilized acylase from Arthrobacter viscosus: A new useful biocatalyst
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Enzymatic synthesis of cephalosporins. The immobilized acylase from Arthrobacter viscosus: A new useful biocatalyst

机译：头孢菌素的酶促合成。粘性节杆菌的固定化酰基转移酶：一种新型有用的生物催化剂

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摘要

The acylase from Arthrobacter viscosus was immobilized, studied in the enzymatic synthesis of some cephalosporins by kinetically controlled N-acylation (kcNa) of different cephem nuclei, and compared with the penicillin G acylase (PGA) from Escherichia coli. The reaction outcomes were dependent on the acylase microbial source and on the type of immobilization support. Generally, both enzymes, when immobilized onto hydrophilic resins such as glyoxyl-agarose (activated with aldehyde groups), displayed higher synthetic performances in comparison with hydrophobic acrylic epoxy-supports like Eupergit C. The kcNa of 7-amino cephalosporanic acid catalyzed by A. viscosus immobilized on glyoxyl-agarose afforded a quantitative conversion in 7-[(1-hydroxy-1-phenyl)-acetamido]-3-acetoxymethyl-Δ3-cephem-4-carboxylic acid, a useful intermediate for the synthesis of Cefamandole and Cefonicid. Similar results were obtained in the synthesis of these cephalosporins by direct acylation of the corresponding 3′-functionalized nucleus. In these reactions, A. viscosus displayed higher synthetic performances than the PGA from E. coli.
机译：固定了节杆菌的酰基转移酶，通过不同头孢烯核的动力学控制的N-酰化（kcNa）在一些头孢菌素的酶促合成中进行了研究，并将其与大肠杆菌中的青霉素G酰基转移酶（PGA）进行了比较。反应结果取决于酰基转移酶的微生物来源和固定化支持物的类型。通常，两种酶固定在亲水性树脂（如乙醛-琼脂糖（经醛基活化））上后，与疏水性丙烯酸环氧载体如Eupergit C相比，显示出更高的合成性能.A催化7-氨基头孢烷酸的kcNa。固定在乙醛-琼脂糖上的粘胶可定量转化为7-[（1-羟基-1-苯基）-乙酰氨基] -3-乙酰氧基甲基-Δ3 -cephem-4-羧酸头孢曼多和头孢尼西德。通过直接酰化相应的3'-官能化核，在合成这些头孢菌素中获得了相似的结果。在这些反应中，粘滞曲霉显示出比大肠杆菌PGA高的合成性能。

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  • 来源
    《Applied Microbiology and Biotechnology》 |2007年第3期|579-587|共9页
  • 作者

    Marco Terreni; Daniela Ubiali; Teodora Bavaro; Massimo Pregnolato; Roberto Fernández-Lafuente; José M. Guisán;

  • 作者单位

    Italian Biocatalysis Center PBL Dipartimento di Chimica Farmaceutica via Taramelli 12 Università degli Studi I-27100 Pavia Italy;

    Italian Biocatalysis Center PBL Dipartimento di Chimica Farmaceutica via Taramelli 12 Università degli Studi I-27100 Pavia Italy;

    Italian Biocatalysis Center PBL Dipartimento di Chimica Farmaceutica via Taramelli 12 Università degli Studi I-27100 Pavia Italy;

    Italian Biocatalysis Center PBL Dipartimento di Chimica Farmaceutica via Taramelli 12 Università degli Studi I-27100 Pavia Italy;

    Departamento de Biocatalisis Instituto de Catalisis-CSIC Campus UAM Cantoblanco 28049 Madrid Spain;

    Departamento de Biocatalisis Instituto de Catalisis-CSIC Campus UAM Cantoblanco 28049 Madrid Spain;

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