Purification and characterization of a novel glucoamylase from Fusarium solani

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• 作者：Haq Nawaz Bhatti ; Mohammad Hamid Rashid ; Rakhsh ; a Nawaz ; Muhammad Asgher ; Raheela Perveen ; Abdul Jabbar
• 关键词：Amyloglucosidase ; Fusarium solani ; Specificity constant ; Purification ; Half-life
• 刊名：Food Chemistry
• 出版年：2007
• 出版时间：2007
• 年：2007
• 卷：103
• 期：2
• 页码：338-343
• 全文大小：380 K

文摘

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 K_cat and K_m were 441/min and 1.9 mg/ml, respectively, for soluble starch, specificity constant (K_cat/K_m) 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⁺.