This chapter reviews and discusses various aspects of texture analysis. The concentration is o the various methods of extracting textural features from images. The geometric, random field, fractal, and signal processing models of texture are presented. The major classes of texture processing pro lems such as segmentation, classification, and shape from texture are discussed. The possible applic tion areas of texture such as automated inspection, document processing, and remote sensing a summarized. A bibliography is provided at the end for further reading.

Texture analysis

This study characterizes biologically active compounds of berry fruits, including non-nutritive compounds such as phenolic compounds, including anthocyanins, phenolic acids, stilbens and tannins, as well as nutritive compounds such as carotenoids and vitamin C. It discusses the biological activity of those compounds, in particular their antioxidant properties and the resulting health benefits.

Bioactive compounds and health-promoting properties of berry fruits: a review.

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.

Functionality of Proteins in Food

Where is MAP Going? A review and future potential of modified atmosphere packaging for meat

Proteins are widely utilized to add functional properties, such as gelling and emulsification to foods. These attributes depend on a number of factors such as molecular structure of the protein, the pH, and the composition of its chemical environment. There is substantial evidence to suggest that the functional properties of food proteins can be further improved by derivatization. Covalent bonding of proteins to polysaccharides and smaller reducing sugars via the Maillard reaction has been shown to alter the functionality of proteins without requiring the addition of chemical reagents. Establishment of a technologically feasible method for preparing the conjugates and optimization of the processing conditions, however, is needed to promote their development as functional food ingredients. This paper provides a state-of-the-art contribution to the impact of the Maillard reaction on protein functionality. It presents a deeper understanding of the influence of processing conditions and reactant formulation on improving desirable properties of proteins. In particular attention is given to how potential improvements could be achieved in the emulsifying, textural, and solubility properties of proteins to add value to commodity food ingredients. Elements that are considered to be critical to the design of functional Maillard conjugates are highlighted and suggestions proposed to facilitate progress in this area.

Creating Proteins with Novel Functionality via the Maillard Reaction: A Review

Sols were prepared from comminuted fish (surimi), beef, pork and turkey muscles. Continuous evaluation of changes in structural rigidity and energy damping during heating of the sols from 3° to 95°C was performed in a nondestructive, temperature-controlled Thermal Scanning Rigidity Monitor. Surimi presented major rigidity transitions at 40°. 48° and 65°C; beef at 43°. 56° and 69°C; pork at 44°, 53° and 69°C; and turkey at 50°, 53° and 79°C. All materials exhibited rapid decrease in energy damping (i.e. increase in elasticity) over a short temperature span. Failure testing of gels indicated differences in strength and deformability. SEM micrographs provided an insight into structural features of the gels.

Thermally Induced Gelation of Selected Comminuted Muscle Systems–Rheological Changes during Processing, Final Strengths and Microstructure

The textural attributes of 8 different heat-induced protein gel preparations evaluated by torsion failure testing and Instron texture profile analysis (TPA) were compared to sensory ratings by a trained texture profile panel. The gels presented a wide range of textural properties as determined by the instrumental and sensory parameters. Among the instrumental parameters, true shear strain at failure was the most frequent and significant predictor of sensory notes. Initial shear modulus and 50% compression force had the poorest correlations with sensory notes. Comparison of the two instrumental tests produced high correlations between shear stress at failure and TPA hardness; true shear strain at failure and TPA cohesiveness; and, initial shear modulus and 50% compression force. High correlations were also observed among various panel notes. Canonical correlation analyses showed that sets of linear combinations of parameters from each one of the 3 tests (torsion, TPA or sensory) were highly correlated to sets from either of the other two. Regression equations relating each of the instrumental tests to sensory notes were developed. Of the torsion failure parameters, the logarithm of true shear strain most commonly appeared in the equations. Of the TPA parameters, cohesiveness and its logarithm were the terms that were most frequent. High R2 values were obtained for regression equations developed for predicting torsion failure parameters based on TPA parameters.

Comparison of two instrumental methods with sensory texture of protein gels

Myosin heavy chain (MHC) content of cooked gels of pollock and croaker surimi decreased during preincubation (“setting”) at temperatures ranging from 4–50C. Decreases in MHC content were attributed to either nondisulfide covalent cross-linking or proteolysis. Depending upon which process dominated at a given temperature, formation of stronger or weaker gels occurred, respectively. Maximum production of cross-linked polymers occurred at the optimum setting temperatures, i.e., at 25C for pollock surimi and 40C for croaker surimi. Subsequent cooking of these set gels at 90C decreased the amount of cross-linked polymers formed at the optimum setting temperature. Addition of free lysine-HCl inhibited formation of cross-linked polymers of MHC during setting and the increase in cooked gel strength for both species. This supports published evidence that cross-linking of MHC during setting may be of the e-amino-(γ-glutamyl) lysine I type, mediated by a transglutaminase enzyme.

Nondisulfide covalent cross-linking of myosin heavy chain in "setting" of Alaska pollock and Atlantic croaker surimi

The effects of cyclic freezing and thawing upon the quality of frozen surimi of two species were studied with respect to sol viscosity, sol rigidity changes during thermal processing and structural failure properties of the cooked gel. A torsion test, used to determine the strength of gels subjected to different thermal histories, revealed that increasing the number of freeze-thaw cycles reduced the strength and deformability of both sand trout and Alaska pollack surimis. Continuous monitoring of sol rigidity during thermal processing showed little changes in thermal transition temperatures caused by freeze-thaw abuse for either surimi but shifts occurred in overall rigidity levels. Particularly dramatic changes were induced in the Alaska pollack rigidity thermogram. The rigidity thermograms of sand trout and Alaska pollack were significantly different, as were their responses to freeze-thaw abuse and low temperature (4°C and 40°C) pretreatments.

Effects of Freeze‐Thaw Abuse on the Viscosity and Gel‐Forming Properties of Surimi from Two Species

Fish pastes were prepared from comminuted fish muscles after washing with water to remove water‐soluble proteins. The pastes were made with 2% salt and adjusted to a 78% moisture content. Shear moduli and energy damping were monitored continuously during heating of the raw paste from 5 to 90°C using a special temperature‐controlled shear fixture (TSRM) in a universal testing machine. The shear modulus‐temperature relationship had peaks at approximately 13 and 37°C and began a permanent increase at about 47°C. Rigidity was also heating rate dependent. Apparent energy loss, (hysteresis area)/(work of deformation), increased slightly from 10 to 25°C reaching about 38% after which the loss decreased rapidly to 50°C and then more slowly to 70°C reaching approximately 8%. Structural failure of the cooked product (gel) was evaluated using torsion and uniaxial compression tests. True shear stresses and true shear strains at failure were not significantly different comparing torsion and uniaxial compression althou...

Tyre C. Lanier

Papers

Thermally Induced Gelation of Selected Comminuted Muscle Systems–Rheological Changes during Processing, Final Strengths and Microstructure

Comparison of two instrumental methods with sensory texture of protein gels

Nondisulfide covalent cross-linking of myosin heavy chain in "setting" of Alaska pollock and Atlantic croaker surimi

Effects of Freeze‐Thaw Abuse on the Viscosity and Gel‐Forming Properties of Surimi from Two Species

Final Strengths and Rheological Changes During Processing of Thermally Induced Fish Muscle Gels