Glucoamylase: structure/function relationships, and protein engineering

Author:

Sauer Jørgen,Sigurskjold Bent W.,Christensen Ulla,Frandsen Torben P.,Mirgorodskaya Ekaterina,Harrison Matt,Roepstorff Peter,Svensson Birte

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference110 articles.

1. Kinetic studies on gluc-amylase. II. Competition between two types of substrate having α-1,4 and α-1,6 glucosidic linkage;Hiromi;J. Biochem. (Tokyo),1966

2. Kinetic studies on gluc-amylase. 3. The influence of pH on the rates of hydrolysis of maltose and panose;Hiromi;J. Biochem. (Tokyo),1966

3. T.P. Frandsen, H.-P. Fierobe, B. Svensson, Engineering specificity and stability in glucoamylase from Aspergillus niger, in: L. Alberghina (Ed.), Protein Engineering in Industrial Biotechnology, Harwood Academic, Amsterdam, 1999, pp. 189–206.

4. Protein engineering of glucoamylase to improve industrial properties. A Review;Reilly;Starch/Stärke,1999

5. Protein engineering of the relative specificity of glucoamylase from Aspergillus awamori based on sequence similarities between starch-degrading enzymes;Sierks;Protein Eng.,1994

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