ArticlePlants (Basel, Switzerland)2016
Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature.
Article in Plants (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 123 citations in OpenAlex.
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- Nutritional and Functional Potential of Rapeseed and Canola Proteins: Advances in Protein Extraction, Phenolic Removal, and Food Applications.Comprehensive reviews in food science and food safety · 2026Review
- Rapeseed Meal as a Sustainable Source of Proteins, Peptides, and Phenolics: Composition, Interactions, and Functional Potential.Foods (Basel, Switzerland) · 2026Review
- Rapid Protein Extraction from Canola Meal Pre-Treated with Enzymatic Reactive Extrusion.Foods (Basel, Switzerland) · 2026Article
- Mustard derived compounds as insecticides and modulators of human metabolism.Scientific reports · 2026Article
- In Silico Proteomic Profiling and Bioactive Peptide Potential of Rapeseed Meal.Foods (Basel, Switzerland) · 2025Article
- Application of Microorganisms for the Valorization of Side-Products of Rapeseed De-Oiling.Biomolecules · 2025Review
- Optimization of Protein Extraction from Rapeseed Oil Cake by Dephenolization Process for Scale-Up Application Using Artificial Neural Networks.Foods (Basel, Switzerland) · 2025Article
- Investigating the Effects ofmicroPublication biology · 2025Article
- An Exploration of the Biochemistry of Mustard Seed Meals: A Phytochemical and In Silico Perspective.Foods (Basel, Switzerland) · 2024Article
- Characterization of Plant based spray dried powders using oil seed proteins and chokeberry extract from wine byproduct.Scientific reports · 2024Article
- Ultrafiltration of Rapeseed Protein Concentrate: Effect of Pectinase Treatment on Membrane Fouling.Foods (Basel, Switzerland) · 2024Article
- Modulating Weak Protein-Protein Cross-Interactions by the Addition of Free Amino Acids at Millimolar Concentrations.The journal of physical chemistry. B · 2024Article
- A Review of the Utilization of Canola Protein as an Emulsifier in the Development of Food Emulsions.Molecules (Basel, Switzerland) · 2023Review
- Partial characterization of canola (Heliyon · 2023Article
- Review
- Characterization of intrinsic molecular structure spectral profiles of feedstocks and co-products from canola bio-oil processing: impacted by source origin.Animal bioscience · 2023Article
- High-Moisture Shear Processes: Molecular Changes of Wheat Gluten and Potential Plant-Based Proteins for Its Replacement.Molecules (Basel, Switzerland) · 2022Review
- Optimization of Selective Hydrolysis of Cruciferins for Production of Potent Mineral Chelating Peptides and Napins Purification to Valorize Total Rapeseed Meal Proteins.Foods (Basel, Switzerland) · 2022Article
- The Effect of Precipitation pH on Protein Recovery Yield and Emulsifying Properties in the Extraction of Protein from Cold-Pressed Rapeseed Press Cake.Molecules (Basel, Switzerland) · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
The two major storage proteins identified in Brassica napus (canola) were isolated and studied for their molecular composition, structural characteristics and the responses of structural features to the changes in pH and temperature. Cruciferin, a complex of six monomers, has a predominantly β-sheet-containing secondary structure. This protein showed low pH unstable tertiary structure, and distinctly different solubility behaviour with pH when intact in the seed cellular matrix. Cruciferin structure unfolds at pH 3 even at ambient temperature. Temperature-induced structure unfolding was observed above the maximum denaturation temperature of cruciferin. Napin was soluble in a wider pH range than cruciferin and has α-helices dominating secondary structure. Structural features of napin showed less sensitivity to the changes in medium pH and temperature. The surface hydrophobicity (S₀) and intrinsic fluorescence of tryptophan residue appear to be good indicators of cruciferin unfolding, however they were not the best to demonstrate structural changes of napin. These two storage proteins of B. napus have distinct molecular characteristics, therefore properties and functionalities they provide are contrasting rather than complementary.
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