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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
