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Cys155 of 27 kDa maize γ-zein is a key amino acid to improve its in vitro digestibility
- Source :
- FEBS Letters. 580:5803-5806
- Publication Year :
- 2006
- Publisher :
- Wiley, 2006.
-
Abstract
- Twenty-seven kilodalton gamma-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, gamma-kafirin. Therefore, each of the conserved disulfide-bonded Cys' was mutated to create C144A, C148A, C155A, and C156A maize gamma-zein mutants. The C155A showed a remarkable increase in digestibility to proteases - pepsin, chymotrypsin, and trypsin. A high conservation of this Cys among cereal gamma-prolamins indicates the utility of this finding.
- Subjects :
- DNA, Plant
Zein
Molecular Sequence Data
Biophysics
In Vitro Techniques
Zea mays
Biochemistry
Structural Biology
Genetics
medicine
Animals
Humans
Storage protein
Cereal
Amino Acid Sequence
Cysteine
Molecular Biology
Peptide sequence
chemistry.chemical_classification
Chymotrypsin
Base Sequence
biology
Protein
food and beverages
Cell Biology
Trypsin
Recombinant Proteins
Amino acid
Molecular Weight
Amino Acid Substitution
chemistry
Protein body
Digestibility
Mutagenesis, Site-Directed
biology.protein
Digestion
Peptide Hydrolases
medicine.drug
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 580
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....05a4e16caeba5a87eecc2351f7481381