Purification and characterization of a novel glucoamylase from Fusarium solani |
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Authors: | Haq Nawaz Bhatti Mohammad Hamid Rashid Rakhshanda Nawaz Muhammad Asgher Raheela Perveen Abdul Jabbar |
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Affiliation: | 1. Department of Chemistry, University of Agriculture, Faisalabad 38040, Pakistan;2. National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Jhang Road Faisalabad, Pakistan;3. Department of Chemistry, Govt College University, Faisalabad, Pakistan |
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Abstract: | 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+. |
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Keywords: | Amyloglucosidase Fusarium solani Specificity constant Purification Half-life |
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