ASPERGILLUS NIGER K8 was selected from twenty-two fungal ……isolates for α-Amylase production. The crude enzyme was partially purified and precipitated by salting out with ammonium sulphate. The fraction salted out with 60% ammonium sulphate saturation showed the highest specific α-amylase activity with 5.42 folds of purification than that of free extract. The optimum temperature for α-amylase enzyme activity was at 60°C. The enzyme was very stable at 60°C for 1 hr and retained more than 80% of its original activity. The optimum specific activity for A. niger K8 was in a narrow range of pH 5.0-6.0. Alpha amylase enzyme was stable at all pH tested. However, it retains more than 75% of its original activity for 1 h at pH value 5.5.
(2014). Purification and Characterization of Extracellular α-amylase from Aspergillus niger K8. Egyptian Journal of Botany, 54(1), 1-11. doi: 10.21608/ejbo.2014.475
MLA
. "Purification and Characterization of Extracellular α-amylase from Aspergillus niger K8", Egyptian Journal of Botany, 54, 1, 2014, 1-11. doi: 10.21608/ejbo.2014.475
HARVARD
(2014). 'Purification and Characterization of Extracellular α-amylase from Aspergillus niger K8', Egyptian Journal of Botany, 54(1), pp. 1-11. doi: 10.21608/ejbo.2014.475
VANCOUVER
Purification and Characterization of Extracellular α-amylase from Aspergillus niger K8. Egyptian Journal of Botany, 2014; 54(1): 1-11. doi: 10.21608/ejbo.2014.475
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