Egg white

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.

Abstract: Carbon-based photoluminescent nanoparticles have recently received increased interest, owing to their favorable optical properties along with their biocompatibility and low toxicity. Such nascent nanomaterials, the so-called carbon dots (CDs or C-dots), are a promising alternative to more toxic metal-based semiconductor quantum dots (QDs) for applications such as bioimaging. Recent advances in the synthesis of CDs allow them to be formed from fine carbon structures (like graphene and multi-wall carbon nanotubes) by topdown methods, or from chemical precursors (like ammonium citrate and ethylenediaminetetraacetic acid) by bottom-up approaches. Typically, these CDs require surface oxidation and/or further passivation to emit fluorescence, which also makes them hydrophilic. Alternatively, some one-step strategies to fabricate surface-passivated CDs have also been shown. We reported a one-step synthesis of multicolor CDs from pyrolysis of epoxy-enriched polystyrene photonic crystals and their potential for use in light-emitting diodes. Herein, we present a simple and rapid strategy to fabricate CDs from cheap and natural carbon sources and further extend their application as printing “inks”. The fluorescent CDs developed herein have the following notable characteristics: 1) one-step generation in minutes from low-cost, natural, edible chicken eggs by plasma-induced pyrolysis; 2) good amphiphilicity with high solubility in a broad range of aqueous and organic solvents; 3) resistance to acids and bases; 4) versatile applications as fluorescent carbon inks for luminescent patterns. Figure 1 shows the fabrication of egg-derived fluorescent CDs and their application as “inks” for luminescent patterns using inkjet or silk-screen printing. We chose chicken eggs as the starting material to maintain low toxicity and affordability of the final product. Low-temperature plasma with highenergy, inherently charged particles (electrons or cations) and excited neutral species was used to create an active chemical environment for the synthesis of the nanostructures. As shown in Figure 1, the egg was separated into egg white and egg yolk, using an egg-separator, prior to use. A glass dish filled with egg white or yolk was placed between two quartz slides (height= 1.5 cm) of the plasma generator. Subsequently, intense and uniform plasma beams generated from the upper electrode (voltage= 50 V, current= 2.4 A) irradiated the egg samples for 3 min to yield dark black products, referred to as CDpew and CDpey for the plasma-treated egg white and yolk, respectively. The yield of CDs from the egg sample was calculated to be approximately 5.96%. Elemental analysis showed an increase in the carbon content of the products (62.42% for CDpey and 56.75% for CDpew) in comparison to that of the starting material (57.55% for egg yolk and 43.50% for egg white), implying carbonization occurs during the plasma treatment (Supporting Information, Table S1). Significantly, solutions of CDpew and CDpey display bright blue fluorescence under UV light (lex= 302 nm). Figure 2 shows high-resolution transmission electron microscope (HRTEM) images of the CDs. CDpey had uniform dispersion without apparent aggregation and a mean particle diameter (Dp) of 2.15 nm (Figure 2a and Figure S2). Detectable rings in the selected-area electron-diffraction (SAED) pattern revealed the crystalline structure of CDpey (Figure 2a inset). Well-resolved lattice fringes with an interplanar spacing of 0.208 nm were observed (Figure 2b), which is close to the (100) facet of graphite. On the other hand, CDpew was well distributed (Dp= 3.39 nm) and appeared Figure 1. Digital photographs of plasma-induced fabrication of eggderived CDs and their application as fluorescent carbon inks. Egg white or yolk, after a few minutes of plasma treatment under ambient conditions, were transformed into well-defined CDs with bright blue emission under UV light. The CD solutions can also be used as inks for making luminescent patterns by inkjet or silk-screen printing.

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.