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  • Title: Purification and biochemical characterization of a novel mesophilic glucoamylase from Aspergillus tritici WZ99.
    Author: Xian L, Feng JX.
    Journal: Int J Biol Macromol; 2018 Feb; 107(Pt A):1122-1130. PubMed ID: 28951303.
    Abstract:
    Glucoamylase, cleaving the nonreducing end of starch releasing glucose, is an important enzyme in starch processing. The optimal temperature for industrial glucoamylase activity is 60-70°C, which is not compatible with the optimal growth temperature for Saccharomyces cerevisiae. In this study, 26 fungal strains producing amylolytic activities that were more active at 30°C than at 60°C were isolated from 151 environmental samples. Fungal strain WZ99, producing extracellular amylolytic activities with the lowest optimal temperature at 40°C, was identified as Aspergillus tritici by analysis of morphological and molecular data. An extracellular glucoamylase was purified from A. tritici WZ99. The optimal pH of the enzyme was 4.0-5.0 and optimal temperature was 45°C. The glucoamylase was stable at pH 4.5-10.0 and below 40°C. Metal ions at four concentrations did not inhibit the enzyme activity. The glucoamylase contained a catalytic domain belonging to glycosyl hydrolase family 15 and thus was named as AtriGA15A. The enzyme shared the highest identity of 54% with a glucoamylase from Rasamsonia emersonii. This glucoamylase showing excellent comprehensive enzymatic characteristics might have potential applications in starch-based bioethanol production and starch processing.
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