Physical Properties and Structural Changes of Myofibrillar Protein Gels Prepared with Basil Seed Gum at Different Salt Levels and Application to Sausages

The objective of this study was to evaluate physical properties and structural changes of myofibrillar protein gels with basil seed gum (BSG) at different salt levels and develop the low-salt sausages with BSG. Myofibrillar protein (MP) gels were prepared with or without BSG at different salt concentrations (0.15, 0.30, and 0.45 M). Cooking yield (CY, %), gel strength (GS, gf), viscosity, sulfhydryl contents, protein surface hydrophobicity, scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FTIR) of MP were measured. Pork sausages were manufactured with 1% BSG at both low-salt (1.0%) and regular-salt (1.5%) levels. pH, color, expressible moisture (EM, %), CY, textural profile analyses, FTIR, sulfhydryl group, and protein surface hydrophobicity (μg) were measured for analyzing the properties of sausages. The addition of 1% BSG to MP gels increased CY and shear stress. Among treatments with different salt concentrations, MP at 0.30 M salt level with 1% BSG had higher GS than that at 0.15 M salt level with BSG. In microstructure, swollen structures were shown in MP gels with BSG. Although CY of sausage at the low-salt concentration (1.0%) decreased, regardless of the BSG addition, hardness values of sausages with regular-salt level increased with the addition of 1% BSG was added. Protein surface hydrophobicity and sulfhydryl contents of sausages increased with the addition of 1% BSG, resulting in higher hardness and lower springiness than those without BSG. These results suggest that BSG could be used as a water-binding and gelling agent in processed meats.

Coomassie Brilliant Blue-binding: a simple and effective method for the determination of water-insoluble protein surface hydrophobicity

A novel Coomassie Brilliant Blue-binding method, which correlated well with the widely accepted ANS fluorescence method (R = 0.95), was developed to determine the surface hydrophobicity of water-insoluble proteins.

Comparison of Two Methods for the Extraction of Fractionated Rice Bran Protein

Two different methods for extracting fractionated rice bran protein (FRBP) from defatted rice bran were investigated according to the solubility of protein in different extraction solvents. The yields of the obtained proteins and their purity were first compared. Sodium dodecyl sulfate polyacrylamide gel electrophoresis, differential scanning calorimetry, protein surface hydrophobicity, and protein secondary molecular structure analyses were subsequently applied to identify and compare the compositional, structural, and functional characteristics of the obtained proteins. The highest yield (13.8%, w/w) and purity (45–47%) of FRBP products were obtained using 0.4 M NaCl, 80% ethanol, and 0.01 M NaOH as extraction solvents to fractionate albumin, globulin, prolamin, and glutelin. Several good properties were exhibited, including good functionality, specific denaturation temperature, and enthalpy values, for FRBP products prepared by the above method.

Research on Soluble Protein Surface Hydrophobicity of Biomaterial Solution from Soy Protein Isolate - Polysaccharide System

The work attempts to study the surface hydrophobicity (S0) of soy protein isolate（SPI）-guar gum(GG) systems for biomaterial. Effect of four factors on the S0 values of the mixtures were studied. A response surface analysis was carried out using the Box-Behnken Design (BBD)method in order to determine the effects and interactions of pH (6.0, 8.0, 10.0), salt(0.05, 0.15, 0.25M), guar gum(0.10, 0.30, 0.50% w/v) and SPI concentrations (3, 4, 5% w/v) on the S0 values of mixtures. The datas were fitted into second order quadratic model. Salt concentration, pH and SPI concentration, interactions between pH and salt concentration, pH and GG concentration, pH and SPI concentration, GG and SPI concentrations were significant(P<0.05).