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Cys155 of 27 kDa maize γ‐zein is a key amino acid to improve its in vitro digestibility
Author(s) -
Lee Sung-Ho,
Hamaker Bruce R.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.09.033
Subject(s) - storage protein , trypsin , pepsin , biochemistry , chymotrypsin , sorghum , in vitro , disulfide bond , proteases , chemistry , protein quality , amino acid , prolamin , food science , enzyme , biology , agronomy , gene
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.