Functionality of plant proteins : properties, methods of assessment, modifications and applications /

"The book discusses insights into the biological, chemical, and physical principles behind the techno-functional and nutritional properties of proteins, existing methods of functionality assessment, and protein modification for functional enhancement in various food applications. With the curre...

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Bibliographic Details
Corporate Author: ScienceDirect (Online service)
Other Authors: Wanasundara, Janitha P. D. (Editor), Schmitt, Christophe (Editor), Lamsal, Buddhi (Editor)
Format: eBook
Language:English
Published: London : Academic Press, [2024]
Subjects:
Online Access:Connect to the full text of this electronic book
Table of Contents:
  • Front Cover
  • Functionality of Plant Proteins
  • Copyright Page
  • Contents
  • List of contributors
  • Preface
  • Acknowledgments
  • I. Proteins of plant sources and fundamentals of protein product development
  • 1 Fundamentals of proteins from plant sources for sustainable and nutritious foods
  • 1.1 Introduction
  • 1.2 Reasons for increased demand of plant proteins
  • 1.3 Changing dynamics of food protein ingredient industry
  • 1.4 Proteins available from major plant sources
  • 1.4.1 Oil-rich sources
  • 1.4.1.1 Soybean
  • 1.4.1.2 Brassica seeds
  • 1.4.1.3 Other oil-rich sources
  • 1.4.2 Starch-rich sources
  • 1.4.3 Proteins from other plant sources: green leaves and algae
  • 1.5 Classification of plant proteins
  • 1.5.1 Based on solubility
  • 1.5.2 Based on sedimentation coefficient
  • 1.5.3 Based on biological function
  • 1.5.4 Structure-based classification
  • 1.6 Designing sustainable and nutritious food with plant proteins
  • 1.7 Conclusion
  • References
  • 2 Processing of protein ingredients from plant sources
  • 2.1 Introduction
  • 2.2 Plant-based protein ingredients
  • 2.3 Preprocessing of plant substrates for protein ingredients
  • 2.3.1 Dehulling
  • 2.3.2 Milling
  • 2.4 Dry-processing separation methods
  • 2.5 Wet-processing methods
  • 2.5.1 Concentrates
  • 2.5.2 Isolates
  • 2.5.3 pH-modulated aqueous solvent extraction
  • 2.5.3.1 Conventional alkali extraction
  • 2.5.3.2 Acid (low pH) extraction
  • 2.5.4 Saline extraction
  • 2.5.5 Aqueous/organic solvents and reverse micellar extraction
  • 2.6 Novel methods for extraction and preparation of protein-rich ingredients
  • 2.6.1 Substrate modification with electromagnetic waves
  • 2.6.2 Enzyme-assisted aqueous extraction (EAE)
  • 2.6.3 Reverse micellar extraction
  • 2.6.4 Membrane-based concentration of protein
  • 2.7 Common food applications for plant proteins and desired functionality.
  • 2.8 Summary
  • References
  • 3 Functionality of plant proteins and importance of aggregation state
  • 3.1 Introduction
  • 3.2 Importance of protein aggregation state
  • 3.3 Protein bulk properties
  • 3.3.1 Protein solubility
  • 3.3.2 Protein viscosity and gelation
  • 3.4 Protein interfacial properties
  • 3.4.1 Protein emulsification
  • 3.4.2 Protein foam formation
  • 3.5 Other functional properties
  • 3.6 Conclusions
  • References
  • 4 Probing the structure-function relationship of proteins with molecular modeling
  • 4.1 Introduction
  • 4.2 Fundamentals of protein folding and structure
  • 4.2.1 Levels of protein structure
  • 4.2.2 Physiological and technological considerations of protein folding
  • 4.3 Modeling protein structure and functionality
  • 4.3.1 Molecular dynamics
  • 4.3.2 Force fields
  • 4.3.3 Applications of molecular dynamics for the study of food proteins
  • 4.3.3.1 Protein-stabilized emulsions
  • 4.3.3.2 Protein aggregation
  • 4.3.3.3 Modeling of allergens
  • 4.3.3.4 Interaction studies
  • 4.3.4 Protein structure prediction
  • 4.3.4.1 Homology modeling
  • 4.3.4.2 Machine learning approaches
  • 4.4 Conclusions
  • References
  • II. Methods of functionality assessment
  • 5 Hydrodynamic properties I: protein-water interactions, solubility, water adsorption, and wettability
  • 5.1 Introduction
  • 5.2 Protein solubility
  • 5.2.1 Assessment of protein solubility
  • 5.2.1.1 Methods for quantifying total and soluble protein content
  • 5.2.1.2 Nitrogen solubility index
  • 5.2.1.3 Protein dispersibility index
  • 5.2.1.4 Protein or nitrogen solubility with pH change
  • 5.3 Water adsorption/binding
  • 5.3.1 Water adsorption capacity and water hydration capacity
  • 5.3.1.1 Water hydration capacity determination of protein materials
  • 5.3.1.2 Water adsorption (holding) capacity determination of pulse flours and protein materials
  • 5.3.2 Wettability.
  • 5.3.2.1 Methods of assessing wettability
  • 5.4 Associated challenges of determination methods
  • References
  • 6 Protein-water-protein interaction: viscosity and gelation
  • 6.1 Introduction
  • 6.2 Protein unfolding and aggregation upon heating
  • 6.3 Molecular interactions related to protein viscosity and gelation
  • 6.3.1 Hydrogen bonds
  • 6.3.2 Hydrophobic interactions
  • 6.3.3 Electrostatic interactions
  • 6.3.4 Disulfide bonds
  • 6.4 Characterization of protein gel properties
  • 6.4.1 Critical gel concentration
  • 6.4.2 Morphology
  • 6.4.3 Gel mechanical properties
  • 6.4.4 Rheological properties
  • 6.4.5 Water-holding capacity and syneresis
  • 6.5 Head-induced gelation
  • 6.5.1 Effect of globulin protein type
  • 6.5.2 Effect of protein concentration
  • 6.5.3 Effect of temperature
  • 6.5.4 Effect of pH and ionic strength
  • 6.6 Nonthermal coagulation/gelation
  • 6.6.1 Acid-induced gelation
  • 6.6.2 Salt-induced gelation
  • 6.6.3 Enzyme-mediated gelation
  • 6.7 Plant protein gel applications as animal protein alternatives
  • 6.7.1 Plant-based meat analogs
  • 6.7.2 Plant-based milk analogs
  • 6.7.3 Plant-based egg analogs
  • 6.8 Conclusions
  • References
  • 7 The interfacial activity of plant proteins: theory, assessment, and application in emulsion development
  • 7.1 Introduction
  • 7.2 Theory of surface and interfacial tension
  • 7.3 Kinetics of interfacial activity of plant proteins
  • 7.4 Interfacial activity assessment methods
  • 7.4.1 Determination of plant protein's oil-water interfacial tension
  • 7.4.2 Determination of the interfacial structure of plant proteins
  • 7.4.3 Determination of the interfacial strength of plant proteins
  • 7.5 Application of plant protein's interfacial activity in emulsification
  • 7.5.1 Challenges associated with plant protein's emulsification behavior
  • 7.5.2 Development of plant protein-stabilized emulsions.
  • 7.5.3 Assessment of plant protein's emulsification ability
  • 7.5.4 Methodologies to determine the stability of plant protein-based emulsions
  • 7.6 Conclusion
  • Acknowledgments
  • References
  • 8 Hydrophobic/hydrophilic surface activity II: foaming properties (air/water interface stabilization)
  • 8.1 Introduction
  • 8.2 Hydrophobic/hydrophilic surface activity of plant-based proteins
  • 8.2.1 Factors influencing plant-based protein hydrophobic/hydrophilic foaming surface activity
  • 8.3 Preparation of plant-based protein foams and assessment of their properties
  • 8.4 Assessment of foam
  • 8.4.1 Direct methods for foam assessment
  • 8.4.2 Indirect methods for foaming assessment
  • 8.4.3 Foam stability measurements
  • 8.4.3.1 Factors affecting foam stability
  • 8.5 Conclusion
  • Acknowledgments
  • Author Contributions
  • Conflict of Interest
  • References
  • 9 Hydrophobic/hydrophilic surface activity III: interactions with other micro- and macromolecules
  • 9.1 Introduction
  • 9.2 Changing the surface activity of proteins with phytochemicals
  • 9.2.1 Surface activity of proteins
  • 9.2.2 Interaction with phytochemicals
  • 9.2.2.1 Origin of the phytochemicals
  • 9.2.2.2 Methods to assess phytochemical interactions with proteins
  • 9.2.2.3 Noncovalent protein modification with phenolic compounds and effect on surface activity
  • 9.2.2.4 Covalent protein modification with phenolic compounds and effect on surface activity
  • 9.2.2.5 Protein modification with flavor compounds and effect on surface activity
  • 9.2.2.5.1 Organosulfur compounds
  • 9.2.2.5.2 Aldehydes
  • 9.2.3 Controversial results and multicomponent mixtures
  • 9.3 Potential applications of modified proteins in food
  • 9.3.1 The potential of native plant proteins
  • 9.3.2 Toward multicomponent ingredients
  • 9.3.3 Functionality of ingredients with bioactive substances
  • 9.4 Conclusion.