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Food proteins are of great interest, not only because of their nutritional importance and their functionality in foods, but also for their detrimental effects. Although proteins from milk, meats (including fish and poultry), eggs, cereals, legumes, and oilseeds have been the traditional sources of protein in the human diet, potentially any proteins from a biological source could serve as a food protein. The primary role of protein in the diet is to provide the building materials for the synthesis of muscle and other tissues, and they play a critical role in many biological processes. They are also responsible for food texture, color, and flavor. Today, food proteins are extracted, modified, and incorporated into processed foods to impart specific functional properties. They can also have adverse effects in the diet: proteins, such as walnuts, pecans, almonds, and cashews, soybean, wheat, milk, egg, crustacean, and fish proteins can be powerful allergens for some people. Applied Food Protein Chemistry is an applied reference which reviews the properties of food proteins and provides in-depth information on important plant and animal proteins consumed around the world. The book is grouped into three sections: (1) overview of food proteins, (2) plant proteins, and (3) animal proteins. Each chapter discusses world production, distribution, utilization, physicochemical properties, and the functional properties of each protein, as well as its food applications. The authors for each of the chapters are carefully selected experts in the field. This book will be a valuable reference tool for those who work on food proteins. It will also be an important text on applied food protein chemistry for upper-level students and graduate students of food science programs.
Properties and uses of gelatin; Whey proteins; Egg protein; Industrial soya protein technology; Leaf protein production and use; The laeather industry; Applications of blood proteins; Processes and equipment for protein by-products in the meat industry; Utilisation of waste protein sources; Industrial gel filtration of proteins; Large-scale enzyme purification.
Food proteins are of great interest, not only because of their nutritional importance and their functionality in foods, but also for their detrimental effects. Although proteins from milk, meats (including fish and poultry), eggs, cereals, legumes, and oilseeds have been the traditional sources of protein in the human diet, potentially any proteins from a biological source could serve as a food protein. The primary role of protein in the diet is to provide the building materials for the synthesis of muscle and other tissues, and they play a critical role in many biological processes. They are also responsible for food texture, color, and flavor. Today, food proteins are extracted, modified, and incorporated into processed foods to impart specific functional properties. They can also have adverse effects in the diet: proteins, such as walnuts, pecans, almonds, and cashews, soybean, wheat, milk, egg, crustacean, and fish proteins can be powerful allergens for some people. Applied Food Protein Chemistry is an applied reference which reviews the properties of food proteins and provides in-depth information on important plant and animal proteins consumed around the world. The book is grouped into three sections: (1) overview of food proteins, (2) plant proteins, and (3) animal proteins. Each chapter discusses world production, distribution, utilization, physicochemical properties, and the functional properties of each protein, as well as its food applications. The authors for each of the chapters are carefully selected experts in the field. This book will be a valuable reference tool for those who work on food proteins. It will also be an important text on applied food protein chemistry for upper-level students and graduate students of food science programs.
The second edition of Structure in Protein Chemistry showcases the latest developments and innovations in the field of protein structure analysis and prediction. The book begins by explaining how proteins are purified and describes methods for elucidating their sequences of amino acids and defining their posttranslational modifications. Comprehensive explanations of crystallography and of noncovalent forces-ionic interactions, hydrogen bonding, and the hydrophobic effect-act as a prelude to an exhaustive description of the atomic details of the structures of proteins. The resulting understanding of protein molecular structure forms the basis for discussions of the evolution of proteins, the symmetry of the oligomeric associations that produce them, and the chemical, mathematical, and physical basis of the techniques used to study their structures. The latter include image reconstruction, nuclear magnetic resonance spectroscopy, proton exchange, optical spectroscopy, electrophoresis, covalent cross-linking, chemical modification, immunochemistry, hydrodynamics, and the scattering of light, X-radiation, and neutrons. These procedures are applied to study the folding of polypeptides and the assembly of oligomers. Biological membranes and their proteins are also discussed. Structure in Protein Chemistry, Second Edition, bridges the gap between introductory biophysical chemistry courses and research literature. It serves as a comprehensive textbook for advanced undergraduates and graduate students in biochemistry, biophysics, and structural and molecular biology. Professionals engaged in chemical, biochemical, and molecular biological research will find it a useful reference.
In recent years, interest in proteins has surged. This resurgence has been driven by the expansion of the post-genomic era when structural genomics and proteomics require new techniques in protein chemistry and new applications of older techniques. Protein chemistry methods are used by nearly every discipline of biomedical research. Many techniques
Techniques in Protein Chemistry IV compiles papers presented at the Sixth Protein Society Symposium held in San Diego, California in 1992. This book discusses the mass spectrometry in protein sequence and structural investigations; site specific heterogeneity of N-linked oligosaccharides on recombinant human erythropoietin; and modification of thiophosphorylated proteins with extrinsic probes. The cysteine and tryptophan amino acid analysis of ABRF92-AAA; development of separation strategies for proteins by capillary electrophoresis; and peptide mapping of 2-D gel proteins by capillary HPLC are also elaborated. This text likewise covers the single syringe-pump solid-phase protein sequencer; hydrophobic contact density distribution functions; and application of chemical shift calculation to protein structure determination by NMR. This publication is valuable to biologists and students concerned with the developments in mass spectrometry of proteins.
Praise for the Series:"The mainly sharp scientific focus of this set of snapshots is a credit to both the contricutors and the editorial team."--Biotechnology and Applied Biochemistry Techniques in Protein Chemistry VIII is the latest volume in this successful series. As a valuable bench-top reference tool for protein chemists, the ten section sof the book are divided by subject area to show the reader which techniques are currently applied to particular problems in protein science. This approach reflects current trends in which specific instruments and methodologies are used in several different areas. * * The book features the latest advances in protein chemistry methodologies in the following areas:* Protein sequencing and amino acid analysis* Mass spectral analysis of peptides and proteins* Posttranslational processing* High-sensitivity protein and peptide separations* Protein folding and NMR* Functional domain analysis* Protein design and engineering* Three-dimensional protein structure
Physical Principles and Techniques of Protein Chemistry, Part B deals with the theories and application of selected physical methods in protein chemistry evaluation. This book is divided into seven chapters that cover the ultracentrifugal analysis, light scattering, infrared (IR) methods, nuclear magnetic resonance (NMR) spectroscopy, and differential thermal analysis of protein properties. This text first describes the fundamental ideas and methodology of sedimentation analysis of ideal noninteracting solutes and the problems of nonideality and solute-solute interaction. This book then deals ...