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Purification and biochemical characterisation of glucoamylase from a newly isolated Aspergillus niger: Relation to starch processing.

Authors :
Bagheri, Ahmad
Khodarahmi, Reza
Mostafaie, Ali
Source :
Food Chemistry. Oct2014, Vol. 161, p270-278. 9p.
Publication Year :
2014

Abstract

Highlights: [•] The purified glucoamylase was a 57–62kDa polypeptide with pI 4.3–4.4. [•] Optimum temperature/pH, K m, V max and k cat of the enzyme were 70°C, 5, 0.33 (mgml−1), 0.095 (Uμg−1 min−1) and 158.3 (S−1), respectively. [•] Fe3+, Al3+ and Hg2+ inhibited, and Ag2+, Ca2+, Zn2+, Mg2+, Cd2+ ions and EDTA did not inhibit the enzyme considerably. [•] The purified enzyme may be useful for industrial starch processing. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
03088146
Volume :
161
Database :
Academic Search Index
Journal :
Food Chemistry
Publication Type :
Academic Journal
Accession number :
96028372
Full Text :
https://doi.org/10.1016/j.foodchem.2014.03.095