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Adsorption isotherms of the Aspergillus niger glucoamylases I and II on the anionic exchanger DEAE–Toyopearl 650
Author(s) -
Soriano R,
Bautista L F,
Martínez M,
Aracil J
Publication year - 1999
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(199903)74:3<199::aid-jctb42>3.0.co;2-b
Subject(s) - adsorption , aspergillus niger , ion exchange , chemistry , langmuir , chromatography , langmuir adsorption model , nuclear chemistry , chemical engineering , thermodynamics , ion , biochemistry , organic chemistry , physics , engineering
In this paper, the ion exchange isotherms of the two isoenzymes of glucoamylase from Aspergillus niger (named glucoamylase I and glucoamylase II) on the resin DEAE–Toyopearl 650 are presented and fitted to the Langmuir model and Henry's Law model, respectively. Furthermore, a comparative study between the adsorption behaviour of both isoenzymes has been performed which also includes the comparison between the monocomponent and bicomponent isotherms. © 1999 Society of Chemical Industry