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Purification and Characterization of Recombinant Cel7A from Maize Seed


The corn grain biofactory was used to produce Cel7A, an exo-cellulase (cellobiohydrolase I) from Hypocrea jecorina. The enzymatic activity on small molecule substrates was equivalent to its fungal counterpart. The corn grain-derived enzyme is glycosylated and 6 kDa smaller than the native fungal protein, likely due to more sugars added in the glycosylation of the fungal enzyme. Our data suggest that corn seed-derived cellobiohydrolase (CBH) I performs as well as or better than its fungal counterpart in releasing sugars from complex substrates such as pre-treated corn stover or wood. This recombinant protein product can enter and expand current reagent enzyme markets as well as create new markets in textile or pulp processing. The purified protein is now available commercially.

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This study was supported by a Phase 1 Small Business Innovation Research Grant from the National Institute for Food and Agriculture (ARKW-2011-00108).

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Correspondence to Elizabeth E. Hood.

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Hood, N.C., Hood, K.R., Woodard, S.L. et al. Purification and Characterization of Recombinant Cel7A from Maize Seed. Appl Biochem Biotechnol 174, 2864–2874 (2014).

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  • Cel7A
  • Recombinant protein
  • Cellobiohydrolase I
  • Protein purification
  • Cellulase
  • Biomass conversion