RECOVERY OF FREE ENZYMES FROM PRODUCT LIQUORS BY BIO-AFFINITY ADSORPTION - TRYPSIN BINDING BY IMMOBILIZED SOYBEAN INHIBITOR

被引:16
作者
HALLING, PJ
DUNNILL, P
机构
[1] Department of Chemical and Biochemical Engineering, University College London, London, WC1E 7JE, Torrington Place
来源
EUROPEAN JOURNAL OF APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 1979年 / 6卷 / 03期
关键词
D O I
10.1007/BF00508091
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
Soybean trypsin inhibitor immobilised to sub-micron ferrite particles functions as an affinity adsorbent for trypsin and the adsorbed enzyme may be recovered following elution in dilute acid. Trypsin can be adsorbed from casein solutions that is has digested. Equilibrium is reached in under 2 min with an effective dissociation constant as low as 10-7 M, allowing recoveries of more than 90% of added enzyme under realistic conditions. These results suggest that bioaffinity adsorbents could be used to recover an enzyme that has converted a macromolecular substrate. The operation of such a process is discussed, and some interactions are described that could be used with suitably high affinity adsorbents for other enzymes. © 1979 Springer-Verlag.
引用
收藏
页码:195 / 205
页数:11
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