ArticlePlant cell reports2014
Co-suppression of synthesis of major α-kafirin sub-class together with γ-kafirin-1 and γ-kafirin-2 required for substantially improved protein digestibility in transgenic sorghum.
Article in Plant cell reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Advances in Extraction, Structure, and Physiochemical Properties of Sorghum Kafirin for Biomaterial Applications: A Review.Journal of functional biomaterials · 2024Review
- Prediction of available energy and amino acid digestibility of Chinese sorghum fed to growing-finishing pigs.Journal of animal science · 2023Article
- Prospects of microgreens as budding living functional food: Breeding and biofortification through OMICS and other approaches for nutritional security.Frontiers in genetics · 2023Review
- Large and stable genome edits at the sorghum alpha kafirin locus result in changes in chromatin accessibility and globally increased expression of genes encoding lysine enrichment.Frontiers in plant science · 2023Article
- Progress and challenges in sorghum biotechnology, a multipurpose feedstock for the bioeconomy.Journal of experimental botany · 2022Review
- Editing of an Alpha-Kafirin Gene Family Increases, Digestibility and Protein Quality in Sorghum.Plant physiology · 2018Article
- Article
- Biofortified Crops Generated by Breeding, Agronomy, and Transgenic Approaches Are Improving Lives of Millions of People around the World.Frontiers in nutrition · 2018Review
- A Comparative Study of Selected Physical and Biochemical Traits of Wild-Type and Transgenic Sorghum to Reveal Differences Relevant to Grain Quality.Frontiers in plant science · 2017Article
- Molecular Approaches to Understand Nutritional Potential of Coarse Cereals.Current genomics · 2016Article
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Authors and funding
9 authors.
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Abstract
key messageCo-suppressing major kafirin sub-classes is fundamental to improved protein digestibility and nutritional value of sorghum. The improvement is linked to an irregularly invaginated phenotype of protein bodies. ABSTRACT: The combined suppression of only two genes, γ kafirin-1 (25 kDa) and γ-kafirin-2 (50 kDa), significantly increases sorghum kafirin in vitro digestibility. Co-suppression of a third gene, α-kafirin A1 (25 kDa), in addition to the two genes increases the digestibility further. The high-digestibility trait has previously only been obtained either through the co-suppression of six kafirin genes (α-A1, 25 kDa; α-B1, 19 kDa; α-B2, 22 kDa; γ-kaf1, 27 kDa; γ-kaf 2, 50 kDa; and δ-kaf 2, 18 kDa) or through random chemical-induced mutations (for example, the high protein digestibility mutant). We present further evidence that suppressing just three of these genes alters kafirin protein cross-linking and protein body microstructure to an irregularly invaginated phenotype. The irregular invaginations are consistent with high pepsin enzyme accessibility and hence high digestibility. The approach we adopted towards increasing sorghum protein digestibility appears to be an effective tool in improving the status of sorghum as a principal supplier of energy and protein in poor communities residing in marginal agro-ecological zones of Africa.
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