Clark Ford Group

Food Science & Human Nutrition / Zoology & Genetics - ISU

Clark F. Ford

Email: cfford@iastate.edu

Group Interests:

Site-Directed and Random Mutagenesis of Glucoamylase

Structure and Function Studies of Glucoamylase

Improvement of Glucoamylase's Industrial Properties:

Substrate Specificity

pH Optimum

Thermal Stability

Ability to Digest Raw Starch Granules

Development of Systems of Fusion Protein Recovery

Some Publications

Graduate Students:

Martin J. Allen - Increase of Aspergillus awamori Glucoamylase Thermal Stability by Proline Substitution and Random Mutagenesis. (mjallen@iastate.edu)

Tsuei-Yun Fang - Modification of Aspergillus awamori Glucoamylase Selectivity and pH optimum by Site-Directed Mutagenesis. (tyfang@iastate.edu)

Saber M. Khan - Structure Determination of the Starch Binding Domain of Aspergillus awamori Glucoamylase by X-Ray Crystallography. (smkhan@iastate.edu)

Yuxing Li - Increase of Aspergillus awamori Glucoamylase Thermal Stability by Proline and Arginine Substitution and Disulphide Bond Engineering. (yxl@iastate.edu)

Some Publications

Note: This list is outdated.

Sierks, M. R., C. Ford, P. J. Reilly, and B. Svensson. (1989) Site-directed mutagenesis at the active site Trp120 of Aspergillus awamori Glucoamylase. Protein Eng. 2: 621-625.

Evans, R., C. Ford, M. Sierks, Z. Nikolov, and B. Svensson. (1990). Deletion analysis of the 0-glycosylated region of Aspergillus Glucoamylase: effect on activity and thermal stability. Gene 91: 131-134.

Chen, L., C. Ford, and Z. Nikolov. (1991). Adsorption to starch of a ß-galactosidase fusion protein containing the starch-binding domain from Aspergillus Glucoamylase. Gene 99: 121-126.

Ford, C., I. Suominen, and C. E. Glatz. (1991). Fusion tails for the recovery and purification of recombinant proteins. Protein Expression and Purification 2: 95-107.

Last Changed: 96/08/05