Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050287 | FEBS Letters | 2006 | 4 Pages |
Abstract
Twenty-seven kilodalton γ-zein is a subclass of the maize zein storage proteins and, due to its localization at the protein body periphery, is critical to digestibility characteristics of all zeins. This protein had low in vitro digestibility, presumably due to its high Cys content (7.35 mol%) that is similar to the hard-to-digest analogous sorghum protein, γ-kafirin. Therefore, each of the conserved disulfide-bonded Cys’ was mutated to create C144A, C148A, C155A, and C156A maize γ-zein mutants. The C155A showed a remarkable increase in digestibility to proteases – pepsin, chymotrypsin, and trypsin. A high conservation of this Cys among cereal γ-prolamins indicates the utility of this finding.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Sung-Ho Lee, Bruce R. Hamaker,