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Physical, Chemical and Biochemical Modifications of Protein-Based Films and Coatings: An Extensive Review

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ABSTRACT

Protein-based films and coatings are an interesting alternative to traditional petroleum-based materials. However, their mechanical and barrier properties need to be enhanced in order to match those of the latter. Physical, chemical, and biochemical methods can be used for this purpose. The aim of this article is to provide an overview of the effects of various treatments on whey, soy, and wheat gluten protein-based films and coatings. These three protein sources have been chosen since they are among the most abundantly used and are well described in the literature. Similar behavior might be expected for other protein sources. Most of the modifications are still not fully understood at a fundamental level, but all the methods discussed change the properties of the proteins and resulting products. Mastering these modifications is an important step towards the industrial implementation of protein-based films.

No MeSH data available.


Reactions catalyzed by transglutaminase, adapted from [30].
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ijms-17-01376-f009: Reactions catalyzed by transglutaminase, adapted from [30].

Mentions: Transglutaminases are enzymes which catalyze the modification of proteins. They catalyze the acyl transfer reaction between the γ-carboxyl group of a glutamine side chain and the ε-amino group of a lysine side chain. Thereby a ε-(γ-glutamyl) lysine bond is formed between the protein chains [248]. This bond, which crosslinks the protein chains, is stable to proteolysis and improves the enzymatic, chemical, and mechanical stability [249]. However, transglutaminase catalyzes three reactions in total (see Figure 9 below).


Physical, Chemical and Biochemical Modifications of Protein-Based Films and Coatings: An Extensive Review
Reactions catalyzed by transglutaminase, adapted from [30].
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5037656&req=5

ijms-17-01376-f009: Reactions catalyzed by transglutaminase, adapted from [30].
Mentions: Transglutaminases are enzymes which catalyze the modification of proteins. They catalyze the acyl transfer reaction between the γ-carboxyl group of a glutamine side chain and the ε-amino group of a lysine side chain. Thereby a ε-(γ-glutamyl) lysine bond is formed between the protein chains [248]. This bond, which crosslinks the protein chains, is stable to proteolysis and improves the enzymatic, chemical, and mechanical stability [249]. However, transglutaminase catalyzes three reactions in total (see Figure 9 below).

View Article: PubMed Central - PubMed

ABSTRACT

Protein-based films and coatings are an interesting alternative to traditional petroleum-based materials. However, their mechanical and barrier properties need to be enhanced in order to match those of the latter. Physical, chemical, and biochemical methods can be used for this purpose. The aim of this article is to provide an overview of the effects of various treatments on whey, soy, and wheat gluten protein-based films and coatings. These three protein sources have been chosen since they are among the most abundantly used and are well described in the literature. Similar behavior might be expected for other protein sources. Most of the modifications are still not fully understood at a fundamental level, but all the methods discussed change the properties of the proteins and resulting products. Mastering these modifications is an important step towards the industrial implementation of protein-based films.

No MeSH data available.