ArticleACS omega2023
Exploring the Amino-Acid Composition, Secondary Structure, and Physicochemical and Functional Properties of Chickpea Protein Isolates.
Article in ACS omega, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 36 citations in OpenAlex.
- Extraction method-dependent structure-function relationships of Astragali complanati semen protein: Implications for its application as a novel plant protein ingredient.Food chemistry: X · 2026Article
- Molecular insights, resistance profiling, and in silico structural modeling of extended-spectrum beta-lactamase-producing E. coli in camels.Veterinary research communications · 2026Article
- Microfluidization-Driven Structural Reorganization and Functional Improvements of Whole Chickpea Flour.Foods (Basel, Switzerland) · 2026Article
- Comprehensive analysis of beta-lactamase genes in clinical strains of Escherichia coli and Klebsiella pneumoniae: molecular characterization, and in Silico predictions.Journal of computer-aided molecular design · 2025Article
- Effects of Maillard Reaction Durations on the Physicochemical and Emulsifying Properties of Chickpea Protein Isolate.Foods (Basel, Switzerland) · 2025Article
- Extraction, Modification, Biofunctionality, and Food Applications of ChickpeaFoods (Basel, Switzerland) · 2024Review
- Unlocking the nutritional potential of chickpea: strategies for biofortification and enhanced multinutrient quality.Frontiers in plant science · 2024Review
- Partial characterization of canola (Heliyon · 2023Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study examined the amino-acid profile, secondary structure, and physicochemical and functional properties of proteins isolated from Anatolian chickpea landraces. Secondary objective of the study was to determine whether a relationship exists between the amino-acid composition and physicochemical and functional properties. Aspartic acid and glutamic acid were the dominant amino acids, while the isolates were deficient in methionine. Secondary structures were determined by Fourier transform infrared spectroscopy, where the β-sheet was shown to be dominant. The denaturation temperature of the isolates was between 87 and 145 °C, and the highest net surface charge (≃28.6 mV) and solubility (∼95.0%) were observed at pH 9.0-10.0. The isolates' water-holding capacity varied between 2.1 and 2.7 g water/g protein, whereas their oil-holding capacity ranged between 3.4 and 4.4 g oil/g protein. Emulsion capacity, emulsifying activity, and the stability indices of isolates were found to be between 401.2 and 469.1 g oil/g protein, 14.5 and 25.7 m
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Registered trials
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