Zein is a prolamine; an alcohol-soluble protein present
in amounts of 2.5-10% （dry basis） in corn. Zein is a
common component used in the manufacture of
plastics, paper coatings, adhesives, substitutes for
shellac, laminated board, and solid color printing films.
Zeins are the main storage proteins found in the seeds
of maize. Following protein translation, the zeins are
stored in the rough endoplasmic reticulum
（ER）-derived protein bodies. The accumulation of zein
in these ER-derived protein bodies results in the
formation of the endosperm - the food storage body of
seeds.
Currently, there are four classes of zein: α, β, γ, and δ.
These classes are expressed sequentially in maize
and are found to interact with each other for stability.
Zein from corn was reported to be approximay
35% α-zein, which includes 2 prominent bands of
22 and 24 kDa. β-zein fails to enter an SDS-PAGE gel
without reduction. Reducing SDS-PAGE analysis
shows that β-zein has 3 major bands of 24, 22, and
14 kDa.1 The amino acid sequences have been
published.2

Precautions and Disclaimer
For Laboratory Use Only. Not for drug, household or
other uses.
Preparation Instructions
Zein is soluble in aqueous alcohols, glycols, ethyl
ether, furfuryl alcohol, tetrahydrofurfuryl alcohol, and
aqueous alkaline solutions of pH 11.5 or greater. Zein
is insoluble in water, acetone, and anhydrous alcohols
（except methanol）.
Storage/Stability
Zein is rapidly denatured in solution and becomes
insoluble.
References
1. Esen, A., Separation of alcohol-soluble proteins
（zeins） from maize into three fractions by
differential solubility. Plant Physiol., 80, 623-627
（1986）.
2. Phillips, R. L., and McClure, B. A., Elevated
protein-bound methionine in seeds of a maize line
resistant to lysine plus threonine. Cereal Chem.,
62, 213-218 （1985）.