کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1190595 | 963535 | 2007 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Purification and characterization of a novel glucoamylase from Fusarium solani Purification and characterization of a novel glucoamylase from Fusarium solani](/preview/png/1190595.png)
Thermostable enzymes are currently being investigated to improve industrial processes of starch saccharification. A novel glucoamylase was purified to electrophoretic homogeneity from the culture supernatant of Fusarium solani on a fast protein liquid chromatographic system (FPLC). The recovery of glucoamylase after gel filtration on FPLC was 31.8% with 26.2-fold increase in specific activity. The enzyme had a molecular mass of 40 kDa by SDS-PAGE and 41 kDa by gel filtration. The glucoamylase exhibited optimum activity at pH 4.5. The Kcat and Km were 441/min and 1.9 mg/ml, respectively, for soluble starch, specificity constant (Kcat/Km) was 232. The enzyme was thermally stable at 50 °C and retained 79% activity after 60 min at this temperature. The half-life of the enzyme was 26 min at 60°C. The enzyme was slightly stimulated by Cu2+ and Mg2+ and strongly inhibited by Hg2+, Pb2+, Zn2+, Ni2+ and Fe3+.
Journal: Food Chemistry - Volume 103, Issue 2, 2007, Pages 338–343