With the knowledge of the amino acid sequences of two maize zein proteins (apparent molecular weights of 19,000 and 22,000), a structural model is proposed for their molecular conformation. The circular dichroic spectrum taken in the 190-240 nm range for a zein protein mixture in methanol solution showed the zein secondary structure to be largely helical. The polar, hydrophobic, and turn charac...

For biomedical applications such as soft tissue engineering, plant proteins are becoming increasingly attractive. Zein, a class of prolamine proteins found in corn, offers excellent properties for application in the human body, but has inferior mechanical properties and lacks aqueous stability. In this study, electrospun scaffolds from neat zein and zein blended with prepolymer and mildly cross...

Cereal Chem. 83(5):565-568 Traditionally, zein is isolated and recovered from corn gluten meal (GCM) using aqueous alcohol as the solvent. Recovery of zein from this solvent is inconvenient and costly. Zein is insoluble in 100% ethanol at room temperature, but it is soluble at 120°C in ethanol. Absolute ethanol effectively extracted zein from CGM, distillers dried grains (DDG), and ground corn....

Zeins, the maize (Zea mays) prolamin storage proteins, accumulate at very high levels in developing endosperm in endoplasmic reticulum membrane-bound protein bodies. Products of the multigene a-zein families and the single-gene g-zein family are arranged in the central hydrophobic core and the cross-linked protein body periphery, respectively, but little is known of the specific roles of family...

Soybean (Glycine max (L.) Merr.) is an important protein source in human diets and animal feeds. The sulphur content of soybean seed proteins, however, is not optimal for ration formulations. Thus, increasing the methionine and cysteine content of soybean seed proteins would enhance the nutritional quality of this widely utilized legume. We have earlier reported the isolation of an 11 kDa delta...

Maize transcription factors (TFs) opaque2 (O2) and the O2 heterodimerizing proteins (OHP1 and OHP2) originated from an ancient segmental duplication. The 22-kDa (z1C) and 19-kDa (z1A, z1B, and z1D) α-zeins are the most abundant storage proteins in maize endosperm. O2 is known to regulate α-zein gene expression, but its target motifs in the 19-kDa α-zein gene promoters have not been identified. ...

Defective endosperm* (De*)-B30 is a dominant maize (Zea mays) mutation that depresses zein synthesis in the developing endosperm. The mutant kernels have an opaque, starchy phenotype, malformed zein protein bodies, and highly increased levels of binding protein and other chaperone proteins in the endosperm. Immunoblotting revealed a novel alpha-zein protein in De*-B30 that migrates between the ...

Introduction Zein, a major protein of corn, is conspicuous for its ability to form films. It is relatively hydrophobic, soluble in alcohol-water mixtures (40% 85%) but insoluble in pure water or alcohols. Current structural models of the zein molecule (Argos et al 1982, Matsushima et al 1997) consider zein is formed by nine to ten tandem repeats of α-helical segments aligned in anti-parallel fa...

Zein, the prolamine fraction of maize, is localized in the endosperm in membrane-bound structures called protein bodies, which have polyribosomes on their surfaces. These polysomes or the mRNA fraction isolated from them will direct the synthesis of zein-like proteins in vitro. The in vitro products consist primarily of two molecular weight classes but show considerable charge heterogeneity whe...

The maize (Zea mays) floury1 (fl1) mutant was first reported almost 100 years ago, but its molecular identity has remained unknown. We report the cloning of Fl1, which encodes a novel zein protein body membrane protein with three predicted transmembrane domains and a C-terminal plant-specific domain of unknown function (DUF593). In wild-type endosperm, the FL1 protein accumulates at a high leve...