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. 2022 Oct;41(10):2023-2035.
doi: 10.1007/s00299-022-02906-6. Epub 2022 Aug 2.

Endosperm-specific accumulation of human α-lactalbumin increases seed lysine content in maize

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Endosperm-specific accumulation of human α-lactalbumin increases seed lysine content in maize

Chenwanli Li et al. Plant Cell Rep. 2022 Oct.

Abstract

This study demonstrated high expression and accumulation of human α-lactalbumin in transgenic maize, and significant improvement of lysine content in maize endosperm. As a high-yield crop, lack of lysine in endosperm storage protein is a major defect of maize (Zea mays L.). Specifically expression of foreign proteins is a potential way to improve lysine content in maize endosperm. Human α-lactalbumin is such a protein with high lysine content and high nutritional value. In this study, the codon-optimized human lactalbumin alpha (LALBA) gene was driven by maize endosperm-specific 27 kD γ-zein promoter, and transformed into maize. Five independent transgenic lines were obtained, and LALBA was highly expressed in endosperm in all these lines. Protein assay indicated that human α-lactalbumin was highly accumulated in maize endosperm. Immuno-localization assay indicated that human α-lactalbumin was mainly deposited into the protein body (PB). Protein interaction assay showed that human α-lactalbumin interacted with 16 kD γ-zein, which might lead to its deposition to the PBs. Amino acid analysis of two independent transgenic lines showed significant increase of lysine contents in transgenic endosperm, with 47.26% and 45.15% increase to their non-transgenic seeds, respectively. We obtained transgenic maize with endosperm-specific accumulation of human α-lactalbumin at high level and increased the lysine content in maize endosperm. This study demonstrated an effective way to improve the nutritional value of maize seeds.

Keywords: 16 kD γ-zein; Endosperm; Human α-lactalbumin; Lysine; Protein body; Transgenic maize.

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