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Purification and biochemical characterisation of glucoamylase from a newly isolated Aspergillus niger: Relation to starch processing.
- 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]
- Subjects :
- *GLUCOAMYLASE
*ASPERGILLUS niger
*STARCH
*POLYPEPTIDES
*ENZYME kinetics
*FOOD science
Subjects
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