Enzyme-catalyzed gel formation of gelatin and chitosan: potential for in situ applications

Chen, Tianhong; Embree, Heather; Brown, Eleanor M.; Taylor, Maryann M.; Payne, Gregory F.

doi:10.1016/s0142-9612(03)00096-6

Cited by 338 publications

(235 citation statements)

References 87 publications

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“…Tyrosinases and laccases are capable of converting low-molecular weight phenols or accessible Tyr residues of proteins into quinones-reacitve species capable for non-enzymatic reactions with nucleophiles, such as reactive amino groups of other amino acid residues, without disruption of gelatines coil to helix transitions because of only 0,3% of Tyr residues in gelatine and their location outside of the Gly-X-Y tripeptide repeat region being responsible for gelatine's helix formation (Chen et al, 2003), and thus forming quiet weak gels because of the same reasons. Transglutaminase catalyses the cross-linking of gelatine by formation of isopeptide bonds between the -carbonyl group of a Glu residue and -amino group of Lys residue, and one molecule of ammonia per cross-link as by-product (Chen et al, 2003;Bertoni et al, 2006;Crescenzi et al, 2002). Presumably transglutaminase-catalyzed cross-linking occurs in the tripeptide repeat region that is responsive for gelatine's helix forming ability (Chen et al, 2003).…”

Section: Wwwintechopencommentioning

confidence: 99%

“…Transglutaminase catalyses the cross-linking of gelatine by formation of isopeptide bonds between the -carbonyl group of a Glu residue and -amino group of Lys residue, and one molecule of ammonia per cross-link as by-product (Chen et al, 2003;Bertoni et al, 2006;Crescenzi et al, 2002). Presumably transglutaminase-catalyzed cross-linking occurs in the tripeptide repeat region that is responsive for gelatine's helix forming ability (Chen et al, 2003). The acyl-transfer enzyme catalyzes transamidation reactions that lead to the formation of N--( -glutamyl)lysine cross-links in proteins (Crescenzi et al, 2002).…”

Section: Wwwintechopencommentioning

confidence: 99%

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Collagen- vs. Gelatine-Based Biomaterials and Their Biocompatibility: Review and Perspectives

Gorgieva¹,

Kokol²

2011

Biomaterials Applications for Nanomedicine

242

250

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Section: Wwwintechopencommentioning

confidence: 99%

Section: Wwwintechopencommentioning

confidence: 99%

Collagen- vs. Gelatine-Based Biomaterials and Their Biocompatibility: Review and Perspectives

Gorgieva¹,

Kokol²

2011

Biomaterials Applications for Nanomedicine

242

250

View full text Add to dashboard Cite

“…Also, it is highly expressed in drug-resistant cancer cells (Kim et al 2006;Mehta et al 2004). Other studies reported the use of TGase for grafting of gelatin or ovalbumin with chitosan to prepare functional biomaterials (Chen et al 2003;Di Pierro et al 2007). Commercial application of TGases has been constantly increased at a rising rate, in particular for the development of new vaccination strategies in infectious and viral infections.…”

Section: Pharmacological Application Of Tgasementioning

confidence: 99%

Transglutaminases: recent achievements and new sources

Martins

Matos

Costa

et al. 2014

Appl Microbiol Biotechnol

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Transglutaminases are a family of enzymes (EC 2.3.2.13), widely distributed in various organs, tissues, and body fluids, that catalyze the formation of a covalent bond between a free amine group and the γ-carboxamide group of protein or peptide-bound glutamine. Besides forming these bonds, that exhibit high resistance to proteolytic degradation, transglutaminases also form extensively cross-linked, generally insoluble, protein biopolymers that are indispensable for the organism to create barriers and stable structures. The extremely high cost of transglutaminase of animal origin has hampered its wider application and has initiated efforts to find an enzyme of microbial origin. Since the early 1990s, many microbial transglutaminase-producing strains have been found, and production processes have been optimized. This has resulted in a rapidly increasing number of applications of transglutaminase in the food sector. However, applications of microbial transglutaminase in other sectors have also been explored, but in a much lesser extent. Our group has identified a transglutaminase in the oomycete Phytophthora cinnamomi, which is able to induct defense responses and disease-like symptoms. In this mini-review, we report the achievements in this area in order to illustrate the importance and the versatility of transglutaminases.

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“…24 Enzymes have also been shown to promote material assembly. For example, Hu and Messersmith have used transglutaminase as a gelation agent in the assembly of hydrogels 25 whilst peroxidases 26 and tyrosinases 27 have also been used.…”

Section: Introductionmentioning

confidence: 99%

Enzymatically Triggered, Isothermally Responsive Polymers: Reprogramming Poly(oligoethylene glycols) To Respond to Phosphatase

et al. 2015

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(2015) Enzymatically-triggered, isothermally responsive polymers : re-programming poly(oligoethylene glycols) to respond to phosphatase. Biomacromolecules . 71881. http://dx.doi.org/10.1021/acs.biomac.5b00929 Permanent WRAP url: http://wrap.warwick.ac.uk/71881 Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work of researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-forprofit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. Publisher's statement:"This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biomacromelecules copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/abs/10.1021/acs.biomac.5b00929 see http://pubs.acs.org/page/policy/articlesonrequest/index.html]." A note on versions:The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP url' above for details on accessing the published version and note that access may require a subscription. By fine-tuning the density of phosphate groups on the backbone, it was possible to induce an isothermal transition: A change in solubility triggered by removal of a small number of phosphate esters from the side chains activating the LCST-type response. As there was no temperature change involved, this serves as a model of a cell-instructed polymer response.Finally, it was found that both polymers were non cytotoxic against MCF-7 cells (at 1 mg.mL -1 ), which confirms promise for biomedical applications.3

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Enzyme-catalyzed gel formation of gelatin and chitosan: potential for in situ applications

Cited by 338 publications

References 87 publications

Collagen- vs. Gelatine-Based Biomaterials and Their Biocompatibility: Review and Perspectives

Collagen- vs. Gelatine-Based Biomaterials and Their Biocompatibility: Review and Perspectives

Transglutaminases: recent achievements and new sources

Enzymatically Triggered, Isothermally Responsive Polymers: Reprogramming Poly(oligoethylene glycols) To Respond to Phosphatase

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