Modification of Gelatin by Reaction with 1,6‐Diisocyanatohexane

Bertoldo, Monica; Bronco, Simona; Gragnoli, Tania; Ciardelli, Francesco

doi:10.1002/mabi.200600215

Cited by 36 publications

(16 citation statements)

References 14 publications

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“…The presence of reactive functional groups in the amino acid side chain of proteins allows cross-linking via chemical reactions with, e.g., acid, alkali or formaldehyde, glutaraldehyde, glyoxal or diisocyanate [70][71][72]. In addition some enzymes like transglutaminase can crosslink protein by catalyzing acyl-transfer reactions between α-carboxyamide groups of glutaminase residues (acyl donor) and ε-amino groups of lysine residues (acyl acceptor), resulting in the formation of ε-(α-glutaminyl) lysine intra and intermolecular bonds [73].…”

Section: Protein Modification To Control and Optimize Film-formationmentioning

confidence: 99%

State of the Art in the Development and Properties of Protein-Based Films and Coatings and Their Applicability to Cellulose Based Products: An Extensive Review

et al. 2015

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Abstract:There is increasing research towards the substitution of petrochemicals by sustainable components. Biopolymers such as proteins, polysaccharides, and lipids derive from a variety of crop sources and most promisingly from waste streams generated during their processing by the agro food industry. Among those, proteins of different types such as whey, casein, gelatin, wheat gluten, soy protein or zein present a potential beyond the food and feed industry for the application in packaging. The general protein hydrophilicity promotes a good compatibility to polar surfaces, such as paper, and a good barrier to apolar gases, such as oxygen and carbon dioxide. The present review deals with the development of protein-based coatings and films. It includes relevant discussion for application in paper or board products, as well as an outlook on its future industrial potential. Proteins with suitable functionalities as food packaging materials are described as well as the different technologies for processing the coatings and the current state of the art about the coating formulations for selectively modulating barrier, mechanical, surface and end of life properties. Some insights onto regulations about packaging use, end of life and perspectives of such natural coating for decreasing the environmental impact of packages are given.

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Section: Protein Modification To Control and Optimize Film-formationmentioning

confidence: 99%

State of the Art in the Development and Properties of Protein-Based Films and Coatings and Their Applicability to Cellulose Based Products: An Extensive Review

et al. 2015

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“…These methods comprise reaction with enzymes such as transglutaminase, [11][12][13][14] phenolics 15 such as tannins, [16][17][18][19][20][21][22][23] aldehydes, isocyanates, carbodiimides, epoxides, and genipin. 24,25 The two first methods appeared the most appropriate and it is well established that transglutaminase catalyses the transamidation reaction between the side chains of lysine and glutamine residues of the gelatine to generate strong amide linkages. [11][12][13][14] The modification of gelatine with phenolics such as tannins occurs via a complex combination of hydrogen bonding, ionic interactions and hydrophobic interactions.…”

Section: Gelatine and Gelatine Modification Methodsmentioning

confidence: 99%

Towards greener stone shot and stone wool materials: binder systems based on gelatine modified with tannin or transglutaminase

et al. 2018

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In the pursuit of greener stone wool and related materials, the development, study and discussion of strong binder systems for such materials based on gelatine modified with tannin or transglutaminase are presented. The first systematic studies and direct comparisons of gelatines with four different gel strengths modified with 3-50% chestnut tree tannin or transglutaminase are presented and discussed.The development of these non-toxic, biopolymer-based binder systems was achieved using composite bars comprising stone shots with submillimeter diameters as a versatile model for stone wool. Contrary to conventional binder systems, the gelatine-based binder systems were able to cure at ambient temperature, and increased unaged and aged mechanical strengths combined with decreased binder solubility were generally observed as a function of increased gel strength and viscosity of the gelatine component.Several of the compositions resulted in mechanical strengths before and after ageing treatments that were within the range of conventional binder systems. Intriguingly, the gelatine-based binder compositions generally appeared less sensitive towards ageing treatment than conventional binders and in several cases even displayed mechanical strengths after ageing treatments that were at a similar level or better than the corresponding unaged strengths. The developed binder systems thus displayed unprecedented "self-healing" properties. The first DMA studies of cross-sections of the composite bars showed that these binder systems could withstand temperatures well above those required and/or commonly encountered in for example the production and general use of stone wool products. The first SEM studies of the composite bars revealed that the binders created a honeycomb-like structure around the stone shots with several thinner bridging points between adjacent stone shots. The development of this highly promising new generation of bio-inspired binder technologies is expected to enable the manufacture of greener stone wool and related materials through the use of non-toxic and natural components that enable an environmentally improved route to these materials via the reduction of adverse environmental effects such as high energy consumption and emissions during the curing process.

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“…Gelatin nanoparticles (GNPs) are usually stabilized by crosslinking with glutaraldehyde, glyoxal, carbodiimide, genipin, transglutaminase and reduced sugars . A crosslinker links gelatin chains to each other . In consequence, the particles maintain their structural integrity (stability) in aqueous environment, since the gelatin chains are tied together by strong covalent bonds .…”

Section: Introductionmentioning

confidence: 99%

Stabilization of Gelatin Nanoparticles Without Crosslinking

Khan

Schneider

2014

Macromol. Biosci.

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Gelatin nanoparticles can be stabilized by entrapping them in Eudragit E100 nanospheres. The size of the nanospheres was dependent on the homogenization speed, producing nanospheres of 433 nm (8000 rpm) and 176 nm (15000 rpm). The nanoparticle morphology was critically dependent on Eudragit E100 concentration; with 2% Eudragit E 100 nanospheres showed spherical depressions (pores) of around 90 nm on the surface. The number of porous particles decreased from 68% to 5% when Eudragit1 E 100 concentration was increased to 6%, which in turn improved gelatin entrapment from 55% to 93% respectively. Additionally, the initial burst release of gelatin was decreased from 30% to 10% respectively.

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Modification of Gelatin by Reaction with 1,6‐Diisocyanatohexane

Cited by 36 publications

References 14 publications

State of the Art in the Development and Properties of Protein-Based Films and Coatings and Their Applicability to Cellulose Based Products: An Extensive Review

State of the Art in the Development and Properties of Protein-Based Films and Coatings and Their Applicability to Cellulose Based Products: An Extensive Review

Towards greener stone shot and stone wool materials: binder systems based on gelatine modified with tannin or transglutaminase

Stabilization of Gelatin Nanoparticles Without Crosslinking

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