INTERACTION OF INVERTASE WITH POLYELECTROLYTES

被引:16
作者
DAUTZENBERG, H [1 ]
KOTZ, J [1 ]
PHILIPP, B [1 ]
ROTHER, G [1 ]
SCHELLENBERGER, A [1 ]
MANSFELD, J [1 ]
机构
[1] MARTIN LUTHER UNIV,INST BIOCHEM,DEPT ENZYMOL,O-4010 HALLE,GERMANY
关键词
INVERTASE; POLYELECTROLYTES; POLYAMPHOLYTES;
D O I
10.1002/bit.260380909
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
In connection with our work on polyelectrolyte complex formation with polyampholytes, the interaction between invertase and several linear polyelectrolytes has been investigated by means of turbidimetry, light scattering measurements, and determination of the enzyme activity. Polyelectrolyte complex formation of invertase was shown to occur with cationic polyelectrolytes only. The light-scattering data yield information on aggregation and disaggregation processes in complex formation. As indicated by our results, only a part of the protein molecules is engaged in this Coulombic interaction, and this part shows a rather small enzyme activity only. Thus, a direct interaction between invertase and a cationic polyelectrolyte is no effective approach to enzyme binding, but a complete immobilization of invertase can be achieved via an "inclusion flocculation" with a symplex formed by interaction between an anionic and a cationic linear polyelectrolyte or via immobilization in symplex microcapsules.
引用
收藏
页码:1012 / 1019
页数:8
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