Clark Ford
Iowa State University
46 Papers
927 Citations
Clark Ford is an academic researcher from Iowa State University. The author has contributed to research in topics: Aspergillus awamori & Thermostability. The author has an hindex of 24, co-authored 46 publications.
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Papers
Fusion tails for the recovery and purification of recombinant proteins
TL;DR: Fusion tails can be used to promote secretion of target proteins and can also provide useful assay tags based on enzymatic activity or antibody binding, and have potential for enhancing recovery using economical recovery methods that are easily scaled up for industrial downstream processing.
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Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori
TL;DR: Differences in substrate activation energies between Glu180----Gln and wild-type glucoamylases indicate that GLU180 binds D-glucosyl residues in subsite 2, and Glu179 and Asp176 are proposed as the general catalytic acid and base of pKa 5.9 and 2.7 respectively.
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Substitution of asparagine residues in Aspergillus awamori glucoamylase by site-directed mutagenesis to eliminate N-glycosylation and inactivation by deamidation
TL;DR: The mutant lacking the N-glycan linked to Asn-395 was synthesized very slowly, and was more associated with cell membrane components and susceptible to proteinase degradation than were wild-type or other mutant glucoamylases.
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Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production of Aspergillus awamori glucoamylase
TL;DR: Observations suggest that alpha-helix rigidity can affect reversible and irreversible glucoamylase stability differently, that the effects of multiple mutations within one alpha- Helix to improve stability are not always additive and that even single mutations can strongly affect extracellular enzyme production.
Site-directed mutagenesis at the active site Trp120 of Aspergillus awamori glucoamylase
TL;DR: It is suggested that Trp120 from a distant subsite is crucial for the stabilization of the transition-state complex in subsites 1 and 2 of the active site.
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