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
Other Authors: Wanasundara, Janitha P. D. (Editor), Schmitt, Christophe (Editor), Lamsal, Buddhi (Editor)
Format: Electronic eBook
Language:English
Published: London : Academic Press, [2024]
Subjects:
Online Access:ScienceDirect
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245 0 0 |a Functionality of plant proteins :  |b properties, methods of assessment, modifications and applications /  |c edited by Janitha P.D. Wanasundara, Christophe Schmitt, Buddhi P. Lamsal. 
260 |a London :  |b Academic Press,  |c [2024] 
300 |a 1 online resource 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
504 |a Includes bibliographical references and index. 
520 |a "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 current market demand for protein ingredients, several lesser-known sources are now being utilized to develop new protein ingredients and products. These new proteins are intended to replaced, partially or wholly, traditional proteins such as egg, milk, meat, soy, and vital gluten. Depending on the source and processing into ingredients, the ability of these proteins to satisfy techno-functional and nutritional requirements in the final food product may differ. Science-based knowledge is needed in the area of protein functionality for making decisions along the value chain, from production on the land to processing and formulation" -- back cover. 
505 0 |a 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. 
505 8 |a 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. 
505 8 |a 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. 
505 8 |a 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. 
650 0 |a Food  |x Composition. 
650 0 |a Food  |x Protein content. 
650 6 |a Aliments  |x Teneur en protéines.  |0 (CaQQLa)201-0013069 
650 7 |a Food  |x Composition  |2 fast  |0 (OCoLC)fst00930485 
650 7 |a Food  |x Protein content  |2 fast  |0 (OCoLC)fst00930580 
700 1 |a Wanasundara, Janitha P. D.,  |e editor.  |1 https://id.oclc.org/worldcat/entity/E39PBJv8F73hc4rktPwTGdGmBP 
700 1 |a Schmitt, Christophe,  |e editor.  |1 https://id.oclc.org/worldcat/entity/E39PBJcwGdH39K6MFYMT9rRYfq 
700 1 |a Lamsal, Buddhi,  |e editor.  |1 https://id.oclc.org/worldcat/entity/E39PCjvYqG9gV3WH7TG8Cw9mBd 
776 0 8 |c Original  |z 0323917216  |z 9780323917216  |w (OCoLC)1375551707 
856 4 0 |3 ScienceDirect  |u https://www.sciencedirect.com/science/book/9780323917216