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Purification of Cyclodextrin‐Glycosyltransferase Enzyme by Affinity Chromatography
Author(s) -
László E.,
Bánky B.,
Seres G.,
Szejtli J.
Publication year - 1981
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19810330808
Subject(s) - affinity chromatography , chromatography , enzyme , chemistry , cyclodextrin , yield (engineering) , homogeneous , hydrolysis , sepharose , biochemistry , materials science , physics , metallurgy , thermodynamics
Cyclodextrin‐glycosyltransferase (CGT) enzyme can be separated by affinity chromatography from hydrolytic enzymes with high efficiency and simultaneously a 113 fold purification has been achieved. The affine gel contained α‐cyclodextrin coupled to Sepharose 6B. This is a one step method for purification and concentration of the CGT enzyme content of the fermentation broths of Bac. macerans with 90–92% yield. The enzyme proved to be homogeneous by gel electrophoresis; molecular mass is 79000 Dalton.