Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii.
作者： Bjarne R. Nielsen , Jan Lehmbeck , Torben P. Frandsen
DOI: 10.1016/S1046-5928(02)00505-3
关键词: Amylopectin 、 Heterologous expression 、 Hydrolase 、 Aspergillus niger 、 Isomaltose 、 Biology 、 Biochemistry 、 Thermostability 、 Talaromyces 、 Maltose
摘要: The gene encoding a thermostable glucoamylase from Talaromyces emersonii was cloned and, subsequently, heterologously expressed in Aspergillus niger. This encodes 618 amino acid long protein with calculated molecular weight of 62,827Da. T. fall into glucoside hydrolase family 15, showing approximately 60% sequence similarity to A. enzyme shows high specific activity towards maltose, isomaltose, and maltoheptaose, having 3-6-fold elevated k(cat) compared niger glucoamylase. showed significantly improved thermostability half life 48h at 65 degrees C 30% (w/v) glucose, 10h for ability the hydrolyse amylopectin is glucoamylase, giving significant higher final glucose yield temperatures. increased thermal stability thus reflected industrial performance, allowing operate temperature than enzyme.
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