Article3 Biotech2017
Structure and function of seed storage proteins in faba bean (Vicia faba L.).
Article in 3 Biotech, 2017. 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, 52 citations in OpenAlex.
- Industrial-scale fractionation of fava bean, chickpea, and red lentil: A comparative analysis of composition, antinutrients, nutrition, structure, and functionality.Current research in food science · 2025Article
- Faba Bean Processing: Thermal and Non-Thermal Processing on Chemical, Antinutritional Factors, and Pharmacological Properties.Molecules (Basel, Switzerland) · 2023Review
- Green Alternatives as Antimicrobial Agents in Mitigating Periodontal Diseases: A Narrative Review.Microorganisms · 2023Review
- Antibacterial peptide fractions from chia seeds (Journal of food science and technology · 2022Article
- Legume Seed Protein Digestibility as Influenced by Traditional and Emerging Physical Processing Technologies.Foods (Basel, Switzerland) · 2022Review
- Review
- Functionality of oat fiber concentrate and faba bean protein concentrate in plant-based substitutes for minced meat.Current research in food science · 2022Article
- Functional and Rheological Properties ofBiomolecules · 2021Article
- Identification and Quantification of Major Faba Bean Seed Proteins.Journal of agricultural and food chemistry · 2020Article
- Genetic relationship study of some Vicia species by FISH and total seed storage protein patterns.Journal, genetic engineering & biotechnology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein subunit is the most important basic unit of protein, and its study can unravel the structure and function of seed storage proteins in faba bean. In this study, we identified six specific protein subunits in Faba bean (cv. Qinghai 13) combining liquid chromatography (LC), liquid chromatography-electronic spray ionization mass (LC-ESI-MS/MS) and bio-information technology. The results suggested a diversity of seed storage proteins in faba bean, and a total of 16 proteins (four GroEL molecular chaperones and 12 plant-specific proteins) were identified from 97-, 96-, 64-, 47-, 42-, and 38-kD-specific protein subunits in faba bean based on the peptide sequence. We also analyzed the composition and abundance of the amino acids, the physicochemical characteristics, secondary structure, three-dimensional structure, transmembrane domain, and possible subcellular localization of these identified proteins in faba bean seed, and finally predicted function and structure. The three-dimensional structures were generated based on homologous modeling, and the protein function was analyzed based on the annotation from the non-redundant protein database (NR database, NCBI) and function analysis of optimal modeling. The objective of this study was to identify the seed storage proteins in faba bean and confirm the structure and function of these proteins. Our results can be useful for the study of protein nutrition and achieve breeding goals for optimal protein quality in faba bean.
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