Reviews the physiochemical properties of the main food proteins and explores the interdependency between the structure-function relationship of specific protein classes and the processing technologies applied to given foods. The book offers solutions to current problems related to the complexity of food composition, preparation and storage, and includes such topics as foams, emulsions, gelation by macromolecules, hydrolysis, microparticles/fat replacers, protein-based edible films, and extraction procedures.

Functionality of Food Proteins: Mechanisms, Modifications, Methods of Assessment and Applications provides researchers and users of plant-based proteins with the latest developments on their functionality at the molecular and ingredient level, and in food applications. The book discusses 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. With market demand for protein ingredients, several lesser known sources are being utilized to develop new protein ingredients and products, with some intended to replace, 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. - Provides fundamentals of the properties that contribute to functionality (nutritional and techno-functional properties) of proteins in food systems and their relationship to protein molecular structure - Describes fundamentals of the assessment of functional properties of protein with existing definitions and food systems - Explores fundamentals of modification strategies employed to alter nutritional and techno-functional properties to enhance value of proteins in food - Includes examples of plant protein-based products (in food systems) in which the role of nutritional and techno-functional properties is described

Understanding of the interactions of milk proteins in complex food systems continues to progress, resulting in specialized milk-protein based applications in functional foods, and in protein ingredients for specific health applications. Milk Proteins is the first and only presentation of the entire dairy food chain – from the source to the nutritional aspects affecting the consumer. With focus on the molecular structures and interactions of milk proteins in various processing methods, Milk Proteins presents a comprehensive overview of the biology and chemistry of milk, as well as featuring the latest science and developments. Significant insight into the use of milk proteins from an industry viewpoint provides valuable application-based information. Those working with food and nutritional research and product development will find this book useful. - 20% new chapter content — full revision throughout - New chapters address: role of milk proteins in human health; aspects of digestion and absorption of milk proteins in the GIT; consumer demand and future trends in milk proteins; and world supply of proteins with a focus on dairy proteins - Internationally recognized authors and editors bring academic and industrial insights to this important topic

For a long time, the tight junction (TJ) was known to form and regulate the paracellular barrier between epithelia and endothelial cell sheets. Starting shortly after the discovery of the proteins forming the TJ—mainly the two families of claudins and TAMPs—several other functions have been discovered, a striking one being the surprising finding that some claudins form paracellular channels for small ions and/or water. This Special Issue includes 43 articles covering numerous dedicated topics including pathogens affecting the TJ barrier, TJ regulation via immune cells, the TJ as a therapeutic target, TJ and cell polarity, function and regulation by proteins of the tricellular TJ, TJ as a regulator of cellular processes, organ- and tissue-specific functions, TJ as sensors and reacting to environmental conditions, and last but not least, TJ proteins and cancer.

A wide variety of hormones, neurotransmitters and growth factors exert their cellular effects by reacting first with membrane receptors resulting in an increase of intracellular calcium and the cellular response. The calcium signal in the cell is mediated by the high-affinity calcium binding proteins (characterized by the EF-hand structural element), and by the calcium and phospholipid dependent proteins. Many of these have been discovered most recently. Their purification, distribution, protein and gene structures as well as their physiological roles are discussed. The book is of interest to biochemists and molecular biologists as well as to clinicians and the pharmaceutical industry who can apply the results in this field.

More than 20 billion dollars worth of biopharmaceuticals are scheduled to go off-patent by 2006. Given the strong political impetus and the development of technological tools that can answer the questions regulatory authorities may raise, it is inevitable that the FDA and EMEA will allow biogeneric or biosimilar products. Even with all the regulato

For the first time, an entire publication has been dedicated to providing a critical review of the identification and analysis of the milk specific proteins such as lactalbumin, lactoferrin and casein; the non-milk specific proteins such as plasma and membrane proteins; and the minor nitrogen-containing components such as enzymes, hormones, and growth factors. Biological roles, whether nutritional, endocrinological or immunological, of the specific nitrogen compounds in mammary milk production and/or growth and development of the breast-fed infant are also presented. Identification of the molecular weight compounds that have led to questions about their function in milk and their inclusion in modern infant formulas is thoroughly discussed and of great value to scientists in sub-specialties of biochemistry, nutrition, physiology and immunology, as well as to pediatric practitioners with primary interests in the infant food industry, academia, or clinical nutrition. The thoroughness of each chapter, often providing an historical panorama of the specific aspect of milk composition, makes this book useful for both the uninitiated and expert audiences who are interested in advancing their knowledge of human milk biochemistry and its physiological significance to the recipient infant.

This volume covers topics such as the structure and identification of functional domains of G proteins, and activation of G proteins by receptors or other regulators. The text takes an integrated approach to studying common experimental questions at many different levels related to G proteins. Methods related to G proteins using molecular modeling, systems biology, protein engineering, protein biochemistry, cell biology, and physiology are all accessible in the same volume. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant todaytruly an essential publication for researchers in all fields of life sciences.

Techniques in Protein Chemistry III compiles papers presented at the Fifth Protein Society Symposium in Baltimore on June 22-26, 1991. This book discusses the protein and peptide recovery from PVDF membranes; high-sensitivity peptide mapping utilizing reversed-phase microbore and microcolumn liquid chromatography; and capillary electrophoresis for preparation of peptides and direct determination of amino acids. The TFMSA/TFA cleavage in t-Boc peptide synthesis; applications of automatic PTC amino acid analysis; and identification of O-glycosylation sites with a gas phase sequencer are also elaborated. This text likewise covers the conformational stability of the molten globule of cytochrome c and role of aqueous solvation in protein folding. This publication is useful to students and researchers interested in methods and research approaches on protein chemistry.

The word revolution has a number of definitions (The American Heritage Dictionary, 2006). The one most pertinent to this series and volume is 'a sudden or momentous change in a situation'. Recent years have seen an unprecedented explosion of interest in unfolded proteins in all of their various forms. Coupled with this increase in interest we have seen momentous changes in the way unfolded proteins are viewed. Two particular paradigms have come under close scrutiny: unfolded proteins are disordered random coils devoid of persistent structure, and protein function first requires protein structure. The first of these is currently a hotly debated subject. The second paradigm we can safely claim has been overturned. There is a second definition of revolution that is quite relevant to a significant portion of the work reviewed herein, in particular those chapters dealing with local and persistent structure in unfolded proteins. That definition is 'a turning or rotational motion about an axis' (The American Heritage Dictionary, 2006). About four decades ago, Charles Tanford (1968) demonstrated that highly denatured proteins possess hydrodynamic properties consistent with Paul Flory's random coil (Flory, 1969). Given that the Flory random coil definition included the stipulation that conformers making up the denatured state ensemble would differ in energy by just a few kT, there has been the assumption that denatured states must therefore be completely random in nature with no persistent structure or biases towards particular conformers. Notably however, Tanford did note the random coil-like hydrodynamic data he obtained did not necessarily rule out the presence of structure in denatured proteins (Tanford, 1968). Around the same time, Sam Krimm and M. Lois Tiffany noted that the CD spectra they obtained for proteins in the presence of high concentration of chemical denaturants had similarities to spectra obtained for homopolymers of proline, lysine, and glutamic acid in water (Tiffany and Krimm, 1968a, 1968b, 1973, 1974). Homopolymers of these residues were known to adopt the left-handed polyproline II conformation, leading Tiffany and Krimm to hypothesise that highly denatured proteins possess significant polyproline II helix content. Of these two views, that espousing the lack of structure in denatured proteins became more widely adopted and was, over time, adopted as a central paradigm in protein folding. As several of the chapters in this volume note, a Tiffany and Krimm-like view appears to be, to some extent, the more correct one. The level to which it is correct is still unknown, although it is clear that the polyproline II helical conformation is not the only, perhaps not even the most common, persistent conformation present in unfolded proteins. Thus we have come through a full circle or revolution. (from the preface)