Development and characterization of a silica monolith immobilized enzyme micro-bioreactor

被引:41
作者
Kawakami, K [1 ]
Sera, Y [1 ]
Sakai, S [1 ]
Ono, T [1 ]
Ijima, H [1 ]
机构
[1] Kyushu Univ, Fac Engn, Dept Chem Engn, Higashi Ku, Fukuoka 8128581, Japan
关键词
D O I
10.1021/ie049354f
中图分类号
TQ [化学工业];
学科分类号
0817 ;
摘要
Several 10-cm-long capillary tubes [made of poly(ether ether ketone) (PEEK)] with inside diameters of 0.1-2.0 mm were filled with silica monolith-immobilized protease derived by in situ sol-gel transition from a 1:4 mixture of tetramethoxysilane and methyltrimethoxysilane. Transesterification between 20 mM (S)-(-)-glycidol and 0.4 M vinyl n-butyrate in an organic solvent was used as the test reaction. The substrate solution flowed through the column at a flow rate of 0.0004-5.0 mL(.)min(-1). The conversion in the micro-bioreactor was higher than that in the batch reactor at a high liquid flow rate. When three tubes were connected in series, the conversion at a fixed ratio of the mass of the enzyme to the liquid flow rate was increased by approximately 50%, because of the tripling of the flow rate as compared to the case with a single tube. Changes in the tube diameter had no influence on the conversion at a fixed superficial liquid velocity. Further, the conversion increased with a decrease in the enzyme content. These results were ascribed to the apparent effect of liquid-solid mass transfer and were analyzed quantitatively using a simple mathematical model.
引用
收藏
页码:236 / 240
页数:5
相关论文
共 12 条
  • [11] 2-E
  • [12] A packed-bed enzyme mini-reactor for the production of structured lipids using nonimmobilized lipases
    Xu, XB
    Zhou, DQ
    Mu, HL
    Adler-Nissen, J
    Hoy, CE
    [J]. JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 2002, 79 (02) : 205 - 206