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  • 技術(shù)文章

    Technical articles

    當(dāng)前位置:首頁技術(shù)文章玉米蛋白,黍膠質(zhì);玉米朊;玉米醇溶蛋白 寶葉提供

    玉米蛋白,黍膠質(zhì);玉米朊;玉米醇溶蛋白 寶葉提供

    更新時(shí)間:2013-06-03點(diǎn)擊次數(shù):2231

    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).

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