肉の代替品となる筋肉タンパク質を生産するように遺伝子操作されたレタスとタバコの植物(Lettuce and tobacco plants engineered to produce muscle protein for meat alternatives)

2026-08-06 インペリアル・カレッジ・ロンドン(ICL)

遺伝子工学により、レタスとタバコの植物に、牛や豚の筋肉に含まれるミオグロビンを作らせることに成功した。ミオグロビンは肉の赤色やうま味に関係する重要なタンパク質で、植物由来の代替肉に肉らしい風味や色を付与する素材として利用できる可能性がある。研究では葉緑体を利用して植物内でミオグロビンを安定的に生産し、乾燥重量1kg当たりレタスで約810mg、タバコで約800mgを蓄積させた。肉そのものと比べた含有量は少ないものの、植物栽培は畜産より土地・水資源や温室効果ガス排出を抑えられる可能性があり、持続可能な代替タンパク質生産の新たな手段として注目される。

肉の代替品となる筋肉タンパク質を生産するように遺伝子操作されたレタスとタバコの植物(Lettuce and tobacco plants engineered to produce muscle protein for meat alternatives)

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植物葉緑体を用いたミオグロビン肉タンパク質の持続可能な生産 Sustainable production of myoglobin meat protein in plant chloroplasts

Alexia Groff ,Yuhan Lu,,Mistianne Feeney,,Julian P. Whitelegge ,Shengxi Shao,Kyoko Morimoto,Peter Julian Nixon
Frontiers in Plant Science  Published:06 August 2026
DOI:https://doi.org/10.3389/fpls.2026.1876707

Abstract

Alternative routes for producing animal proteins are crucial for reducing the reliance on traditional livestock farming, which contributes significantly to greenhouse gas emissions, deforestation, and water consumption. Myoglobin (Mb) is an important oxygen-binding hemoprotein found in vertebrate muscle which enhances the nutritional and sensorial properties of meat. Due to its unique functionality, Mb has been heterologously expressed in a variety of organisms, although only transient expression in Nicotiana benthamiana has been reported for higher plants. In this study, we used chloroplast transformation technology to express porcine Mb in higher plants (tobacco, a non-edible model plant, and lettuce, an edible host) and bovine Mb in the green alga Chlamydomonas reinhardtii. Mb accumulation was estimated by immunoblotting and found to be much higher in tobacco (2.7% total soluble protein (TSP)) and lettuce (1.5% TSP) than Chlamydomonas reinhardtii (<0.25% TSP). The expression in tobacco chloroplasts is also superior to tobacco nuclear expression (using either the cauliflower mosaic virus 35S promoter or the Arabidopsis thaliana ubiquitin promoter). Total heme levels were elevated in myoglobin-producing mutants compared with control plants, although porcine Mb purified from tobacco leaves exhibited approximately 35% heme-binding (compared with 80% heme-binding in E. coli-expressed Mb), despite being correctly folded, suggesting that heme availability might be a bottleneck. Overall, our work describes the first report of stable Mb production in higher plants and its effect on photosynthesis and heme levels. This provides a foundation for future plant-made animal proteins for food applications.

1202農芸化学
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