Film formation and surface properties of enzymatically crosslinked casein films

Juvonen, Helka; Smolander, Maria; Boer, Harry; Pere, Jaakko; Büchert, Johanna; Peltonen, Jouko

doi:10.1002/app.32943

Cited by 29 publications

(15 citation statements)

References 50 publications

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“…Edible thin films from various different proteins have been prepared by enzyme-catalyzed crosslinking with microbial transglutaminase (Di Pierro et al 2006; Mariniello et al 2010), and recently, also with tyrosinase and laccase (Juvonen et al 2011). For example, films containing transglutaminase-crosslinked whey proteins embedded in a chitosan matrix showed (1) low solubility in water (2) reduced permeability for oxygen, carbon dioxide, and water vapor, and (3) enhanced elongation to break but lower deformability than noncrosslinked films (Di Pierro et al 2006).…”

Section: Formation Of Protein Networkmentioning

confidence: 99%

Enzyme-catalyzed protein crosslinking

Heck

Faccio

Richter

et al. 2012

Appl Microbiol Biotechnol

257

190

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The process of protein crosslinking comprises the chemical, enzymatic, or chemoenzymatic formation of new covalent bonds between polypeptides. This allows (1) the site-directed coupling of proteins with distinct properties and (2) the de novo assembly of polymeric protein networks. Transferases, hydrolases, and oxidoreductases can be employed as catalysts for the synthesis of crosslinked proteins, thereby complementing chemical crosslinking strategies. Here, we review enzymatic approaches that are used for protein crosslinking at the industrial level or have shown promising potential in investigations on the lab-scale. We illustrate the underlying mechanisms of crosslink formation and point out the roles of the enzymes in their natural environments. Additionally, we discuss advantages and drawbacks of the enzyme-based crosslinking strategies and their potential for different applications.

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Section: Formation Of Protein Networkmentioning

confidence: 99%

Enzyme-catalyzed protein crosslinking

Heck

Faccio

Richter

et al. 2012

Appl Microbiol Biotechnol

257

190

View full text Add to dashboard Cite

show abstract

“…21,22 Casein films and coatings are predominantly manufactured by conventional processes, such as solution casting and spin-coating processes. 23,24 Furthermore, they have potential applications in the medical sector, e.g., as biocompatible wound dressing material or in drug delivery systems. 25,26 Structure of casein micelle Over the years, several models for the casein micelle structure have been published and were intensively discussed in the literature.…”

Section: Introductionmentioning

confidence: 99%

The enzyme-mediated autodeposition of casein: effect of enzyme immobilization on deposition of protein structures

2016

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The enzyme-mediated autodeposition on the example of casein is reviewed, and deposition of casein structures is investigated in relation to applied immobilization methods of enzyme. First, casein is described in detail with respect to its structure in aqueous environments, followed by presentation of historical and current nonfood applications of casein. The presented process uses enzymes to trigger deposition of bio-based particles in close proximity to a support surface and allows for a high control over film formation and site-specificity. This is ensured by immobilization of enzyme on the support material. The herein described system is based on casein as protein and chymosin as enzyme. Different immobilization methods are investigated with respect to obtainable casein coatings, layers, and structures. Physical adsorption of enzyme enables the formation of casein coatings with controllable film thickness and is suitable for in situ buildup of adhesive layers due to diffusion of enzyme. The highest control over film formation is provided by covalent attachment of enzyme. Based on the attained results, the enzymemediated autodeposition gives new insights into biological material design. Graphical abstractEnzyme Casein micelle intact Bulk zone (no enzyme) Reaction zone Phe Met Support Support Casein micelle cleaved

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“…On the other hand, chemical methods, such as alkali-treatment or the addition of various cross-linkers, were reported to improve the elongation and strength and decrease the solubility of casein films [22]. Additives, such as stearic acid or various enzymes, were helpful to improve the water-resistance and mechanical properties of casein films, while DL-glyceraldehyde and glutaraldehyde also enhanced the microstructure of glycerol plasticized casein films [13,25,26].…”

mentioning

confidence: 99%

Casein Films: The Effects of Formulation, Environmental Conditions and the Addition of Citric Pectin on the Structure and Mechanical Properties

et al. 2014

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Thin casein films for food packaging applications reportedly possess good strength and low oxygen permeability, but low elasticity and high sensitivity to moisture. Modifying the films to target specific behaviors depending on environmental conditions can enable a variety of commercial applications for casein-based films. The mechanical properties of solvent-cast (15% solids) calcium-caseinate/glycerol films (CaCas:Gly ratio of 3:1) were characterized as a function of processing and environmental conditions, including film thickness, solution formulation and ambient humidity (from 22% to 70% relative humidity (RH) at ~20 °C). At constant RH, the elongation at break (EAB) had a strong positive dependence on the film thickness. When RH increased, the tensile strength (TS) and modulus (E) decreased approximately linearly, while EAB increased. From 0.05% to 1% (w/w) of citric pectin (CP) was then incorporated into CaCas/Gly films following seven different formulations (mixing sequences), to alter the protein network and to evaluate the effects of CP on the tensile properties of CaCas/Gly/CP films. At constant film thickness and ~60% RH, the addition of 0.1% or 1.0% CP to the films considerably increased or decreased EAB, TS and E in different directions and to different extents, depending on the formulation, while optical micrographs also showed vastly differing OPEN ACCESSPolymers 2014, 6 2019 network configurations, suggesting complex formulation-and stoichiometry-dependent casein-pectin interactions within the dried films. Depending on the desired film properties and utilization conditions, pectin may be a useful addition to casein film formulations for food packaging applications.

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Film formation and surface properties of enzymatically crosslinked casein films

Cited by 29 publications

References 50 publications

Enzyme-catalyzed protein crosslinking

Enzyme-catalyzed protein crosslinking

The enzyme-mediated autodeposition of casein: effect of enzyme immobilization on deposition of protein structures

Casein Films: The Effects of Formulation, Environmental Conditions and the Addition of Citric Pectin on the Structure and Mechanical Properties

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