Tatsushi Noutomi

Bio: Tatsushi Noutomi is an academic researcher. The author has contributed to research in topics: Ovalbumin & Conformational change. The author has an hindex of 2, co-authored 2 publications receiving 245 citations.

Thermally induced changes in egg white proteins

Abstract: The heat-induced aggragation of egg white protein and conformational change of heat-denatured protein at a high pH value were investigated. The flexibility, surface hydrophobicity, and changes in sulfhydryl groups were determined.

Emulsifying and structural properties of ovalbumin

Abstract: The emulsifying properties of ovalbumin were investigated, and the relationships between the emulsifying properties and protein structure were also discussed. The emulsifying properties of ovalbumin were dependent on pH, concentration of protein dispersion, oil-phase volume, and presence of salts. The pH was the most important variable in the emulsifying activity. The emulsifying activity of ovalbumin was relatively high in the acidic pH region. The surface hydrophobicity of ovalbumin was greater at acidic pHs than at neutral pHs. No significant difference was found between the secondary structure of ovalbumin at pH 3 and that at pH 7, but microenvironmental changes were shown around the aromatic amino acid residues in acid solution. The line widths of 31P NMR spectra in ovalbumin at pH 3 or 8 suggested that the conformation of ovalbumin was more flexible at acidic pHs than at neutral pHs. Thus, the high emulsifying activity of ovalbumin at acidic phs was assumed to correlate with the greater surface hydrophobicity and flexibility of the molecule.

Recent advances in the understanding of egg white protein functionality

Abstract: Hen egg white proteins have been extensively utilized as ingredients in food processing because of their unique functional properties, such as gelling and foaming. This review article describes the molecular basis for the development of these functional properties during processing, as well as studies of the development of new methods for improving the functional properties of egg white proteins. The theory that egg white proteins are capable of existing in a ‘molten globule state’, which partially explains their functional properties, is also discussed.

Functionality of Proteins in Food

Abstract: References.- 1 Solubility of Proteins.- 1.1 Introduction.- 1.1.1 Factors Affecting Solubility of Proteins.- 1.2 Solubility of Meat and Fish Proteins.- 1.2.1 Solubility of Muscle Proteins.- 1.2.2 Solubility of Stroma Proteins.- 1.2.3 Protein Solubility in Processed Meats.- 1.2.4 Solubility of Blood Proteins.- 1.2.5 The Effect of Heating on Solubility of Proteins.- 1.2.6 The Effect of Freezing and Storage When Frozen on Protein Solubility.- 1.2.7 The Effect of Protein Modification and Irradiation Treatment.- 1.3 Solubility of Milk Proteins.- 1.4 Solubility of Egg Proteins.- 1.5 Solubility of Plant Proteins.- 1.5.1 Soybean Proteins.- 1.5.2 Peanut Proteins.- 1.5.3 Pea and Bean Proteins.- 1.5.4 Sunflower Proteins.- 1.5.5 Corn Proteins.- 1.5.6 Miscellaneous Plant Proteins.- References.- 2 Water Holding Capacity of Proteins.- 2.1 Introduction.- 2.2 The Mechanism of Protein-Water Interaction.- 2.2.1 Factors Influencing Water Binding of Proteins.- 2.3 Water Holding Capacity of Proteins in Meat and Meat Products.- 2.3.1 Water Binding Capacity of Muscle Proteins.- 2.3.2 Factors Influencing Water Binding of Muscle Proteins.- 2.3.3 Water Binding in Comminuted Meat Products.- 2.3.4 Milk Proteins in Comminuted Meats.- 2.3.5 Soy Proteins in Comminuted Meats.- 2.3.6 Corn Germ Protein in Comminuted Meats.- 2.4 Water Holding Capacity of Milk Proteins.- 2.5 Water Holding Capacity of Egg Proteins.- 2.6 Water Holding Capacity of Plant Proteins.- 2.6.1 Soybean Proteins.- 2.6.2 Pea and Bean Proteins.- 2.6.3 Sunflower Proteins.- 2.6.4 Corn Proteins.- 2.6.5 Wheat Proteins.- 2.6.6 Miscellaneous Proteins.- References.- 3 Emulsifying Properties of Proteins.- 3.1 Introduction.- 3.2 Hydrophobic and Hydrophilic Properties of Proteins.- 3.3 Interfacial Film Formation and Properties.- 3.4 Factors Affecting the Emulsifying Properties of Proteins.- 3.4.1 Protein Concentration.- 3.4.2 pH of Medium.- 3.4.3 Ionic Strength.- 3.4.4 Heat Treatment and Other Factors.- 3.5 Emulsion Stability.- 3.6 Measuring Emulsifying Properties.- 3.7 Emulsifying Properties of Meat Proteins and Proteins Utilized as Extenders in Meat Products.- 3.7.1 Protein Functionality in Comminuted Meats.- 3.7.2 Emulsifying Properties of Various Muscular Proteins.- 3.7.3 Emulsifying Properties of Blood Proteins.- 3.8 Functionality of Nonmeat Proteins in Comminuted Meats.- 3.8.1 Milk Proteins.- 3.8.2 Soy Proteins.- 3.8.3 Corn and Wheat Germ Proteins.- 3.9 Milk Proteins as Emulsifiers in Food Systems.- 3.9.1 Emulsifying Properties of Caseins and Caseinates.- 3.9.2 Emulsifying Properties of Whey Proteins.- 3.10 Emulsifying Properties of Egg Proteins.- 3.11 Emulsifying Properties of Plant Proteins.- 3.11.1 Soybean Proteins.- 3.11.2 Pea and Bean Proteins.- 3.11.3 Corn Proteins.- 3.11.4 Miscellaneous Proteins.- References.- 4 Oil and Fat Binding Properties Of Proteins.- 4.1 Introduction.- 4.2 Fat Binding Properties of Proteins of Animal Origin.- 4.2.1 Muscle Proteins.- 4.2.2 Soy Proteins in Comminuted Meats.- 4.2.3 The Effect of Corn Germ Protein Flour on Fat Binding in Ground Beef Patties.- 4.2.4 Milk and Egg Proteins.- 4.3 Fat Binding Properties of Proteins of Plant Origin.- 4.3.1 Soy Proteins.- 4.3.2 Pea, Bean and Guar Proteins.- 4.3.3 Corn Germ Proteins.- 4.3.4 Wheat Proteins.- 4.3.5 Cottonseed Proteins.- 4.3.6 Miscellaneous Proteins.- References.- 5 Foaming Properties of Proteins.- 5.1 Introduction.- 5.2 The Mechanism of Foam Formation.- 5.2.1 Factors Affecting Foam Formation.- 5.2.2 Foam Stability.- 5.3 Milk Proteins.- 5.3.1 Factors Affecting the Foaming Properties of Milk Proteins.- 5.4 Egg Proteins.- 5.4.1 The Effect of Processing on Foaming Properties of Egg Proteins.- 5.5 Blood Proteins and Gelatin.- 5.6 The Foaming Properties of Plant Proteins.- References.- 6 Gelling Properties of Proteins.- 6.1 Introduction.- 6.2 The Mechanism of Protein Gel Formation.- 6.2.1 Heat-Induced Gelation.- 6.2.2 Protein-Water Interaction in Gels.- 6.2.3 Factors Affecting the Properties of Gels.- 6.3 Gelling Properties of Meat Proteins.- 6.3.1 Myofibrillar Proteins.- 6.3.2 Sarcoplasmic Proteins.- 6.3.3 Gelation of Red and White Muscle Proteins.- 6.3.4 Factors Affecting the Gelling Properties of Meat Proteins.- 6.3.5 Myosin Blends with Other Proteins and Lipids.- 6.3.6 Fish Proteins.- 6.3.7 Collagen Gelation.- 6.3.8 Blood Proteins.- 6.4 Gelling Properties of Milk Proteins.- 6.4.1 Gelling Properties of Whey Protein Concentrate, Isolate, and Individual hey Proteins.- 6.4.2 The Effect of Heating and Protein Concentration.- 6.4.3 Gelation of Casein.- 6.4.4 Factors Affecting the Gelling Properties of Milk Proteins.- 6.5 Gelling Properties of Egg Proteins.- 6.5.1 Gelation of Egg White.- 6.5.2 Gelation of Yolk.- 6.6 Gelling Properties of Soy Proteins.- References.

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing.

Abstract: Biomolecular condensates are membraneless intracellular assemblies that often form via liquid-liquid phase separation and have the ability to concentrate biopolymers. Research over the past 10 years has revealed that condensates play fundamental roles in cellular organization and physiology, and our understanding of the molecular principles, components and forces underlying their formation has substantially increased. Condensate assembly is tightly regulated in the intracellular environment, and failure to control condensate properties, formation and dissolution can lead to protein misfolding and aggregation, which are often the cause of ageing-associated diseases. In this Review, we describe the mechanisms and regulation of condensate assembly and dissolution, highlight recent advances in understanding the role of biomolecular condensates in ageing and disease, and discuss how cellular stress, ageing-related loss of homeostasis and a decline in protein quality control may contribute to the formation of aberrant, disease-causing condensates. Our improved understanding of condensate pathology provides a promising path for the treatment of protein aggregation diseases.

Bioactive egg compounds

Abstract: Composition and Extraction of Egg Components.- Composition and Structure of Hen Egg Yolk.- Low-density Lipoproteins (LDL) or Lipovitellenin Fraction.- High-density Lipoproteins (HDL) or Lipovitellin Fraction.- Phosvitin.- Livetin Fractions (IgY).- Lysozyme.- Ovotransferrin.- Ovalbumin and Gene-Related Proteins.- Ovomucin.- Riboflavin-Binding Protein (Flavoprotein).- Avidin.- Proteases.- Antiproteases.- Minor Proteins.- Structure and Formation of the Eggshell.- Eggshell Matrix Proteins.- Function of Eggshell Matrix Proteins.- Use of Egg Compounds for Human Nutrition.- Nutritional Evaluation of Egg Compounds.- Concepts of Hypoallergenicity.- Egg Enrichment in Omega-3 Fatty Acids.- Enrichment in Vitamins.- Enrichment in Selenium and Other Trace Elements.- Use of Eggs for Human/Animal Health and Biotechnology.- Compounds with Antibacterial Activity.- Egg-Protein-Derived Peptides with Antihypertensive Activity.- Use of IgY Antibodies in Human and Veterinary Medicine.- Egg Compounds with Antioxidant and Mineral Binding Properties.- Use of Lecithin and Lecithin Fractions.- Extraction of Several Egg Compounds at a Pilot Scale.- Use of Egg Compounds for Cosmetics and Pharmaceutics.- Use of Egg Compounds for Cryoprotection of Spermatozoa.- Egg-Protein-Based Films and Coatings.- Magnetic Particles for Egg Research.- Avidin-Biotin Technology.