A simple method of affinity chromatography for the purification of glucoamylase obtained from Aspergillus niger C

Optimization of extraction and purification of glucoamylase produced by Aspergillus awamori in solid-state fermentation

“…Hayashida and Teramoto [13] had previously reported the production of three kinds of glucoamylases: GA I (type A: raw starch digesting), GA I' (type B: raw-starch-non-digesting), and GA II (type C) by A. awamori. Paszczyński et al [14] also revealed that A. niger consisted of two major components with estimated molecular weights of 63.5 ± 3 and 57.0 ± 2.5 kDa. Our zymograms study of partially purified glucoamylase obtained after ion exchange chromatography likewise confirmed the enzyme produced by A. awamori existed in three isoforms and that all three forms possessed starch hydrolysis ability (Fig.…”

Various molecular species in glucoamylase from Aspergillus niger.

“…[14][15][16][17][18][19][20][21][22][23][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42][43] and No. 51 -64 were separately pooled, dialyzed, concentrated by ultra filtration, and referred to as A-II, A-III, and A-IV, respectively, after further purification by rechromatography under the same conditions.…”

“…Furthermore, the capacity of the column to absorb the enzyme and its specificity for binding glucoamylase rather than amylases and glucosidases were proved to be far higher than the previously reported affinity columns. [16][17][18][19] Thus, affinity chromatography on acarbose columns has enabled us to purify a large amount of GA without recourse to timeconsuming and multiple step isolation procedures. The affinity chromatographically purified enzyme preparation is also expected to be suitable as a material for further study of the properties of the GAcomponents inclusive not only of the major enzymebut also of the minor ones that have never been characterized.…”

Affinity chromatographic separation of secreted alkaline phosphatase and glucoamylase using reactive dyes

“…Among them, Aspergillus niger is the most widely used one for commercial production. Traditionally, glucoamylase is purified by affinity chromatographic separation using b-cyclodextrin-chitosan [9] or amylopectin [10]. Teotia and co-workers established a one-step purification method by affinity precipitation with alginate [11].…”