Characterization of two forms of glucoamylase from aspergillus niger

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Structure of the catalytic domain of glucoamylase from Aspergillus niger.

Glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides. The G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region. The amino-terminal catalytic domain of the G1 isoform generated by subtilisin cleavage has been cry...

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production and characterization of glucoamylase by aspergillus niger

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Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger.

The catalytic domain of glucoamylases G1 and G2 from Aspergillus niger is produced in vitro in high yield by limited proteolysis using either subtilisin Novo or subtilisin Carlsberg. Purification by affinity chromatography on an acarbose-Sepharose column followed by ion-exchange chromatography on HiLoad Q-Sepharose leads to separation of a number of structurally closely related forms of domain....

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Directed evolution of Aspergillus niger glucoamylase to increase thermostability

Using directed evolution and site-directed mutagenesis, we have isolated a highly thermostable variant of Aspergillus niger glucoamylase (GA), designated CR2-1. CR2-1 includes the previously described mutations Asn20Cys and Ala27Cys (forming a new disulfide bond), Ser30Pro, Thr62Ala, Ser119Pro, Gly137Ala, Thr290Ala, His391Tyr and Ser436Pro. In addition, CR2-1 includes several new putative therm...

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ژورنال

عنوان ژورنال: Carlsberg Research Communications

سال: 1982

ISSN: 0105-1938

DOI: 10.1007/bf02907797