Swelling, Mechanical, and Barrier Properties of Albedo-Based Films Prepared in the Presence of Phaseolin Cross-Linked or Not by Transglutaminase

Mariniello, Loredana; Giosafatto, C. Valeria L.; Pierro, Próspero Di; Sorrentino, Angela; Porta, Raffaele

doi:10.1021/bm100566j

Cited by 37 publications

(20 citation statements)

References 33 publications

(73 reference statements)

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“…Similar changes regarding the barrier properties were observed in thin film preparations of grapefruit albedo homogenates combined with the bean protein phaseolin after transglutaminase-catalyzed crosslinking. However, in contrast to the whey protein films studied by Di Pierro et al (2006), the transglutaminase-treated albedo homogenate–phaseolin films not only revealed higher tensile strength but also an approximately twofold increase in their elasticity (Mariniello et al 2010). …”

Section: Formation Of Protein Networkmentioning

confidence: 91%

“…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%

See 1 more Smart Citation

Enzyme-catalyzed protein crosslinking

Heck

Faccio

Richter

et al. 2012

Appl Microbiol Biotechnol

253

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.

show abstract

Section: Formation Of Protein Networkmentioning

confidence: 91%

Section: Formation Of Protein Networkmentioning

confidence: 99%

Enzyme-catalyzed protein crosslinking

Heck

Faccio

Richter

et al. 2012

Appl Microbiol Biotechnol

253

190

View full text Add to dashboard Cite

show abstract

“…Another interesting protein is phaseolin [255][256][257][258][259], a globular protein from Phaseulus Vulgaris L. and proteins purified from Vicia Ervilia. Many papers have been published recently using as crosslinking agent the enzyme transglutaminase, and as plasticizers glycerol or trehalose with or without different polysaccharides to obtain composite films.…”

Section: Emerging Proteins From Plant Kingdommentioning

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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“…Most of the biodegradable plastics are produced utilizing renewable biomass sources, whereas fossil-fuel plastics (poly-ethylene, -vi- invertebrates and vertebrates [39,41,42,49].…”

mentioning

confidence: 99%

“…It was demonstrated that the enzymecatalyzed formation of protein crosslinks into the film network gener-ally determines a decreased solubility of the bioplastics and increases its capacity to stretch. Concerning the pectin-based materials, the effect of mTG was shown both to significantly increase the barrier properties to both oxygen and carbon dioxide and to confer to these bioplastics a moderate permeability to water vapour [41,42]. These modifications of bioplastics characteristics suggest their possible use in a variety of situations, one of which could be the edible wrapping of high-moisture food to prevent their quality changes.…”

mentioning

confidence: 99%

Promising Perspectives for Transglutaminase In “Bioplastics” Production

Porta¹,

Pierro²,

Sorrentino³

et al. 2011

J Biotechnol Biomaterial

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When Heinrich B. Waelsch [53,13], Laszlo Lorand [33] and John E. Folk [20]-the latter who passed away on Dec 27th 2010 and to whom we wish to dedicate the present Editorial -began to investigate at the middle of the past century on the calcium dependent transamidating activities contained in the guinea pig liver and blood, no one could imagine that transglutaminase (TG, EC 2.3.2.13) would become at the beginning of the new millennium one of the most interesting biocatalyst for industrial applications in several different fields. An accurate historical overview of the first 50 years of TG research was recently reported by Beninati et al. [3] in occasion of the "IX Conference on Transglutaminase and Protein Crosslinking" held in Marrakesh in the early days of September 2007.The complete name of the enzyme, R-glutaminyl-peptide:amineg-glutamyltransferase, indicates that the catalysis consists of the acyl transfer of g-glutamyl residues, present in protein or peptide substrates (acyl donor), to an acyl acceptor substrate, resulting in a variety of different products depending on the involved molecules [21]. The transamidation reaction occurs when the acyl acceptor is either the ε-amino group of an endoprotein lysine residue or a low molecular mass primary amine, generating ε-(g-glutamyl)lysine crosslinked linear or branched homo-and heteropolymers, in the first case, or protein-amino derivatives in the latter. The wide range of interest on TG biological role is mostly related to the existence of multiple molecular forms of the enzyme which are present in different organisms, such as bacteria, plants, Although TG was mostly studied for the ability to post-translationally remodel many different proteins in vivo, its reaction has attracted the attention of many scientists in the last twenty years as an effective way to manipulate the structure of proteins of different origin outside the living cells. Therefore, applied investigations with the different enzyme isoforms have been carried out in different fields, from biomedicine and cosmetics to food, leather, and textile industry [41]. As far as the human health applications, concentrated Factor XIII, a zymogenic form of the enzyme, is used as therapeutic agent to correct blood coagulation in a rare genetic condition due to its deficiency and to reduce bleeding risks [36]. Factor XIII was the first TG isoform used to modify protein and peptide substrates in vitro [45]. In addition, the so-called "tissue" TG (type 2) is an effective biomedical technological tool exploited for the diagnosis of an autoimmune pathology like the celiac disease [15,19]. Also this isoform was extensively tested to modify both structure and biological properties of several polypeptides in vitro [41]. However, both Factor XIII and type 2 TG are not really attractive for industrial uses, since their production is expensive and they cannot be easily manipulated outside of their natural environment. Moreover, further molecular forms of the enzyme extracted from plant or animal tissues were never s...

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Swelling, Mechanical, and Barrier Properties of Albedo-Based Films Prepared in the Presence of Phaseolin Cross-Linked or Not by Transglutaminase

Cited by 37 publications

References 33 publications

Enzyme-catalyzed protein crosslinking

Enzyme-catalyzed protein crosslinking

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

Promising Perspectives for Transglutaminase In “Bioplastics” Production

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