Purification of Cyclodextrin‐Glycosyltransferase Enzyme by Affinity Chromatography | Zendy

László E. | Zendy; Bánky B. | Zendy; Seres G. | Zendy; Szejtli J. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research