Protein solubility (PS) values of different soy protein isolate (SPI) films were determined in water, 0.01 N HCl, 0.01 N NaOH, 4 M urea, and 0.2 M 2-mercaptoethanol. Tensile and color (L, a, and b values) properties of films also were determined. Control films were cast from heated (70 degrees C for 20 min), alkaline (pH 10) aqueous solutions of SPI (5 g/100 mL of water) and glycerin (50% w/w of SPI). Additional films were cast after incorporation of dialdehyde starch (DAS) at 10% w/w of SPI or small amounts of formaldehyde in the film-forming solutions. Also, control film samples were subjected to heat curing (90 degrees C for 24 h), UV radiation (51.8 J/m(2)), or adsorption of formaldehyde vapors. PS of control films was highest (P < 0.05) in 2-mercaptoethanol, confirming the importance of disulfide bonds in SPI film formation. All treatments were effective in reducing (P < 0.05) film PS in all solvents. Both DAS and adsorbed formaldehyde rendered the protein in films practically insoluble in all solvents. Adsorption of formaldehyde vapors and heat curing also substantially increased (P < 0.05) film tensile strength from 8.2 to 15.8 or 14.7 MPa, respectively. However, heat curing decreased (P < 0.05) film elongation at break from 30 to 6%. Most treatments had small but significant (P < 0.05) effects on b color values, with DAS-containing films having the greatest (P < 0. 05) mean b value (most yellowish). Also, DAS-containing, heat-cured, and UV-irradiated films were darker, as evidenced by their lower (P < 0.05) L values, than control films. It was demonstrated that PS of SPI films can be notably modified through chemical or physical treatments prior to or after casting.

SUMMARY: As a means of effective utilization of fish water‐soluble proteins (FWSP), which are mostly discarded into the waste water of seafood processing plants, the development and characterization of edible films from FWSP of blue marlin meat were investigated. The film‐forming solutions were prepared from 3% FWSP solutions at pH 10 with 1.5% glycerol as a plasticizer, followed by heating at 70°C for 15 min. Edible films were successfully prepared by drying the film‐forming solutions at 25°C for 20 h. It was revealed that FWSP had to be denatured somehow to unfold the protein structure, and the interaction of FWSP molecules, particularly through disulfide linkages, was attributed to the formation of films. Transparent edible films thus formed had better flexibility and lower water vapor permeability compared with most of the other protein films.

Films were cast from heated, alkaline aqueous solutions of soy protein (5 g/100 mL water) and glycerin (50% w/w of protein). Control and ultraviolet (UV) irradiated (13.0, 25.9,38.9, 51.8, 77.8, or 103.7 J/m2) films were evaluated for tensile strength (TS), elongation at break (E), water vapor permeability (WVP), and Hunter L, a, and b color values. TS increased (p<0.05) linearly while E decreased linearly with UV dosage. WVP was not affected (P>0.05) by UV irradiation. UV treatment intensified the yellowish coloration of films (increased +b values). SDS‐PAGE patterns for UV‐treated samples revealed bands of aggregates, increasing in intensity with UV dosage, which were absent in control samples. These changes suggested UV‐induced cross‐linking in films.

The functional properties of heat-induced egg white gels were investigated at five pH values. Textural characteristics were determined using the Instron Universal Machine. Hardness, elasticity, cohesiveness, chewiness, and fracturability were maximum at pH 11. Hunter L values were maximum at pH 5 and 7. Microstructure studied with electron microscopy was distinctly different at the five pH values. Alkaline gels showed a fine ordered network that might have contributed to excellent textural characteristics. Water-holding capacity (WHC) was high at alkaline pH, but decreased with addition of 2-mercaptoethanol, suggesting that disulfide bonds were important in egg white gels. Sodium dodecyl sulfate (SDS) improved WHC at pH 7 and 9. No significant correlation was observed between textural profiles and WHC.

The effects of the Maillard reaction on the functional properties of dried egg white (DEW) were investigated. Maillard-reacted DEW (M-DEW) was prepared by storing sugar-preserved DEW (SP-DEW) at 55 degrees C and 35% relative humidity for 0-12 days. The M-DEW developed an excellent gelling property, and hydrogen sulfide production from heat-induced M-DEW gels decreased. Surface sulfhydryl (SH) group content of M-DEW increased while total SH group and alpha-helix contents decreased with increasing heating time in the dry state. Breaking strength, breaking strain, water-holding capacity, and hydrogen sulfide of heat-induced M-DEW gels significantly correlated with surface and total SH group contents in M-DEW. SDS-PAGE revealed that M-DEW proteins were polymerized in which covalent bonds were involved. The present study demonstrated that the Maillard reaction partially unfolds and polymerizes proteins of SP-DEW and, consequently, improved gelling property of SP-DEW under certain controlled conditions.

Films were cast from heated (40 °C for 20 min) alkaline (pH 11.25) aqueous solutions of egg white (EW) solids (9 g/100 mL of water), polyethylene glycol 400 (60% w/w of EW), yolk solids (10% w/w of EW), and dialdehyde starch (DAS) at 0, 2.5, 5, 7.5, or 10% (w/w) of EW. For all types of films, tensile strength (TS), percentage elongation at break (E), Hunter color values (L, a, and b), total soluble matter (TSM) after immersion in water at 25 °C for 24 h, and protein solubility (PS) after immersion for 12 h in buffers (pH 8) containing urea and urea/2-mercaptoethanol were determined. DAS addition increased (P < 0.05) film TS and yellowness (+b values) and reduced (P < 0.05) film TSM and PS in both buffer systems. These modifications in film properties suggested occurrence of cross-linking between EW protein and DAS. This was further supported by SDS−PAGE patterns. Such patterns for DAS-containing films revealed bands of aggregates, increasing in intensity with increasing amounts of DAS, which were absent from patterns of control EW films. Keywords: Egg albumen; protein films; dialdehyde starch; cross-linking

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Films plasticized with polyethylene glycol were cast from alkaline (pH 10.5, 11.0, or 11.5), aqueous egg white (EW) solutions with or without heating (40°C for 30 min). Prior to casting, concentration of surface sulfhydryl (SH) groups was determined and they increased (P < 0.05) (3.81-19.45 mM/g protein) with both pH and heating, presumably due to protein denaturation and cleavage of disulfide (S-S) bonds. Concentration of surface SH groups correlated (P < 0.05) with film tensile strength (r = 0.70), elongation at break (r = 0.86), and film total soluble matter (r = -0.94). Most likely, surface SH groups formed S-S bonds through air oxidation and/or sulfhydryl/disulfide interchange, thus contributing to EW film formation. SDS-PAGE patterns in presence or absence of 2-mercaptoethanol confirmed occurrence of S-S bonding in dried EW films.