Mechanical Properties and Water Vapor Permeability of Edible Films from Whey Protein Isolate and<i>N</i>-Ethylmaleimide or Cysteine

Fairley, Peter; Monahan, Frank J.; German, J. Bruce; Krochta, John M.

doi:10.1021/jf9601731

Cited by 31 publications

(32 citation statements)

References 17 publications

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“…However, our results support the hypothesis that hydrogen bonding plays a major role in the films mechanical properties. These results also corroborate those obtained by Fairly et al [30] who showed that the effects of hydrogen bonding far outweigh those of disulfide bonding in WPI films and that sulfhydryl/disulfide exchange does not significantly determine the films functional properties of, unlike their role in determining the strength of whey protein gels [31]. It should be noted that our values are comparable to those obtained with gelatin films, a biopolymer currently used in biomedical applications [4].…”

Section: Mechanical Propertiessupporting

confidence: 92%

Characterization and evaluation of whey protein-based biofilms as substrates for in vitro cell cultures

et al. 2005

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Section: Mechanical Propertiessupporting

confidence: 92%

Characterization and evaluation of whey protein-based biofilms as substrates for in vitro cell cultures

et al. 2005

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“…The solubility was determined to be 38 ± 5% as shown in table 2. This relative insolubility in water is consistent with the observation that whey protein films are largely insoluble [20]. The high interaction density and the presence of intermolecular covalent bonds or physical knots could be responsible for part of the insolubility of these films.…”

Section: Thickness Density Moisture Content and Solubilitysupporting

confidence: 88%

Production of Artificial Sausage Casings from Whey Proteins

Mubururu¹

2014

IJNFS

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This research and product development work is a contribution to both the Dairy and Meat Industry. The work involved the production of artificial sausage casings from whey proteins. The main objective was to utilize whey, a byproduct from cheese production and produce an edible film which can be utilized as an alternative sausage casing material. The work was based on the whey proteins film forming capabilities. The formation of whey protein-based films mainly involved heat denaturation in aqueous solution at 75 -100°C, which produced intermolecular disulfide bonds, which were responsible for film structure. A plasticizer was added to impart flexibility and extensibility of the edible polymeric film. Addition of a cross-linking agent was for the formation of chemical links between molecular chains to form a threedimensional network of connected molecules. Harvesting of the edible films was done via the casting method.

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“…In particular, unfolding of the native conformation of globular whey proteins at neutral pH leads to exposure of free sulfhydryl groups (SH) and hydrophobic amino acid side-chains, normally occluded within bovine serum albumin (BSA) and lg (Kazmierski & Corredig, 2003;Schmitt et al, 2009;Shimada & Cheftel, 1989). With further heat treatment, free SH may rapidly interchange with existing disulfide bonds to generate new inter-and intramolecular disulfide bonds that will engage toward protein aggregation (Fairley, Monahan, German, & Krochta, 1996;Schokker, Singh, Pinder, & Creamer, 2000). The formation of intermolecular disulfide bonds by sulfhydryldisulfide interchange is considered one of the major mechanisms of protein aggregation, and is mainly governed by formation of lg oligomers that combine into large aggregates (Havea, Singh & Creamer, 2002).…”

Section: Introductionmentioning

confidence: 99%

Influence of moderate electric fields on gelation of whey protein isolate

et al. 2015

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Proteins are one of the food constituents most affected by heating, and some of the changes involve their unfolding, denaturation and gelation. Ohmic heating has often been claimed to improve the quality of foodstuffs due to its uniform heating and (putative) presence of a moderate electric field (MEF). However, this is still subject to discussion, so it is important to determine the effect of ohmic heating and of its MEF upon food constituents. Hence, the aim of this work was to evaluate the effects of MEF on denaturation, aggregation and viscoelastic properties of whey protein isolate (WPI), and compare them with those obtained via conventional heating under identical treatment conditions (up to 30 min at 85 o C). Results have shown that MEF interferes with whey protein unfolding and aggregation pathways at relatively high temperatures. MEF treatments have resulted in WPI solutions possessing more 8 and 10% of native Lactoglobulin and Lactalbumin, respectively, after 30 s of heating at 85 o C, when compared with a conventional heating method. Protein aggregates from MEF-treated WPI solutions presented a maximum increase in size of 78 nm, whereas conventional heating produced an increase of 86 nm. Unlike in conventional heating, aggregation of whey proteins during MEF was not sufficiently strong to form a true elastic gel network, since decreases in both storage and loss modulus were observed following MEF treatment. Our results suggest that MEF may provide a novel method for production of a whey protein matrix with distinctive gel-forming properties.2

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Mechanical Properties and Water Vapor Permeability of Edible Films from Whey Protein Isolate andN-Ethylmaleimide or Cysteine

Cited by 31 publications

References 17 publications

Characterization and evaluation of whey protein-based biofilms as substrates for in vitro cell cultures

Characterization and evaluation of whey protein-based biofilms as substrates for in vitro cell cultures

Production of Artificial Sausage Casings from Whey Proteins

Influence of moderate electric fields on gelation of whey protein isolate

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