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Purification and Characterization of endo ‐ and exo‐lnulinase 1
Author(s) -
Azhari Rosa,
Szlak Alda M.,
Ilan Ehud,
Sideman Samuel,
Lotan Noah
Publication year - 1989
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1989.tb01400.x
Subject(s) - inulinase , inulin , chemistry , enzyme , gel permeation chromatography , glycosidic bond , glycoside hydrolase , chromatography , invertase , affinity chromatography , ion chromatography , ion exchange , biochemistry , organic chemistry , ion , polymer
A crude inulinase preparation, from Aspergillus, was fractioned in a sequence of operations, including ion exchange chromatography on CM‐Sepharose and high‐performance gel permeation chromatography. Two highly purified inulin‐degrading enzymes were thus obtained and some of their characteristics were established. The first enzyme had an endo ‐type activity, a M r of 53,000, and K m = 570 mm (in terms of glycosidic bonds). The second was of the exo ‐type, and has a M r of 81,000 and K m = 60 mm (in terms of inulin chains). The two enzymes are highly activated (up to 20‐fold) by Fe 3+ and partially inhibited by Mn 2+ and Mg 2+ . Both enzymes also exhibit invertase activity.