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Relevant bibliographies by topics / Transglutaminase

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Academic literature on the topic 'Transglutaminase'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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Journal articles on the topic "Transglutaminase"

1

Zilda, Dewi Zeswita. "MICROBIAL TRANSGLUTAMINASE: SOURCE, PRODUCTION AND ITS ROLE TO IMPROVE SURIMI PROPERTIES." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 9, no. 1 (2014): 35. http://dx.doi.org/10.15578/squalen.v9i1.82.

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Transglutaminases (EC 2.3.2.13) have attracted a wide interest from both scientific and appliedpoints of view due to their capacity to cross-link protein substrates. Obtaining transglutaminasesderived from animals are extremely high cost process, which has hampered its wider applicationuntil the discovery of transglutaminase produced by microorganisms. In the early 1990, sincemicrobial transglutaminase have been found, many transglutaminase-producing microbial strainshave been isolated and the enzyme production processes have been optimized. This resulted in the increased uses of transglutamin

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Sidauruk, Santhy Wisuda, Tati Nurhayati, and Untung Trimo Laksono. "Characterization of Endogenous Transglutaminase Enzyme of Yellow Pike Conger’s Liver." Jurnal Pengolahan Hasil Perikanan Indonesia 20, no. 3 (2017): 582. http://dx.doi.org/10.17844/jphpi.v20i3.19816.

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Transglutaminases have been found in various living organism, such as mammals, plants, <br />microorganisms, and marine organisms including fishes. Transglutaminases have many various functions<br />such as food properties, non-food properties and pharmacologies. This research aimed to characterize<br />transglutaminase that obtained from byproducts of yellow pike conger (Congresox talabon) such as<br />catadromous fish of yellow pike conger’s liver. The characteristic of transglutaminase had the possibility<br />to know the optimum condition in application of tra

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Martin, Antonio, Giulia De Vivo, and Vittorio Gentile. "Possible Role of the Transglutaminases in the Pathogenesis of Alzheimer's Disease and Other Neurodegenerative Diseases." International Journal of Alzheimer's Disease 2011 (2011): 1–8. http://dx.doi.org/10.4061/2011/865432.

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Transglutaminases are ubiquitous enzymes which catalyze posttranslational modifications of proteins. Recently, transglutaminase-catalyzed post-translational modification of proteins has been shown to be involved in the molecular mechanisms responsible for human diseases. Transglutaminase activity has been hypothesized to be involved also in the pathogenetic mechanisms responsible for several human neurodegenerative diseases. Alzheimer's disease and other neurodegenerative diseases, such as Parkinson's disease, supranuclear palsy, Huntington's disease, and other polyglutamine diseases, are char

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Sachslehner, Attila Placido, Marta Surbek, Bahar Golabi, et al. "Transglutaminase Activity Is Conserved in Stratified Epithelia and Skin Appendages of Mammals and Birds." International Journal of Molecular Sciences 24, no. 3 (2023): 2193. http://dx.doi.org/10.3390/ijms24032193.

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The cross-linking of structural proteins is critical for establishing the mechanical stability of the epithelial compartments of the skin and skin appendages. The introduction of isopeptide bonds between glutamine and lysine residues depends on catalysis by transglutaminases and represents the main protein cross-linking mechanism besides the formation of disulfide bonds. Here, we used a fluorescent labeling protocol to localize the activity of transglutaminases on thin sections of the integument and its appendages in mammals and birds. In human tissues, transglutaminase activity was detected i

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Indarto, Cahyo, Wahyu Prihanta, and Supriyanto. "The beginning study of transglutaminase from plant origin." E3S Web of Conferences 499 (2024): 01030. http://dx.doi.org/10.1051/e3sconf/202449901030.

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Texture is an important parameter in processed foods such as meatball, sausage and surimi, where it is affected by the protein gel strength. Sodium tripolyphosphate is often used to improve quality of food texture, and even borax which is harmful to health including causing severe dizziness and trouble breathing, is still widely used. This study aims to explore and characterize transglutaminase of plant origin which is safer than gelling chemicals agents in food products. Transglutaminase is an enzime that can modify protein into strong gel by creating cross-linkage among protein chains. Anima

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Cocuzzi, E., M. Piacentini, S. Beninati, and S. I. Chung. "Post-translational modification of apolipoprotein B by transglutaminases." Biochemical Journal 265, no. 3 (1990): 707–13. http://dx.doi.org/10.1042/bj2650707.

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The major form of cross-link found in apolipoprotein B was identified as N1N12-bis-(gamma-glutamyl)spermine, a product known to be formed through the catalytic action of transglutaminases (EC 2.3.2.13). N1-(gamma-Glutamyl)spermine was present in a trace amount but epsilon-(gamma-glutamyl)lysine cross-links, which are formed during fibrin formation in plasma, were not detected. In the presence of catalytic amounts of plasma Factor XIIIa (a thrombin-dependent extracellular transglutaminase) or cellular transglutaminase (a cytosolic enzyme), apolipoprotein B and other plasma apolipoproteins (A-I,

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Dadabay, C. Y., and L. J. Pike. "Purification and characterization of a cytosolic transglutaminase from a cultured human tumour-cell line." Biochemical Journal 264, no. 3 (1989): 679–85. http://dx.doi.org/10.1042/bj2640679.

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Transglutaminases are a family of Ca2(+)-dependent enzymes that catalyse the formation of isopeptide bonds between the side chains of glutamine and lysine residues. The enzymes have been hypothesized to be involved in a wide range of cellular processes, including growth and differentiation and stabilization of the cytoskeleton. The human epidermal carcinoma-cell line, A431 cells, have relatively high amounts of a cytosolic transglutaminase activity that varies upon treatment of the cells with epidermal growth factor. We demonstrate here that this cytosolic activity has the biochemical and immu

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Lerner, Aaron, and Torsten Matthias. "Processed Food Additive Microbial Transglutaminase and Its Cross-Linked Gliadin Complexes Are Potential Public Health Concerns in Celiac Disease." International Journal of Molecular Sciences 21, no. 3 (2020): 1127. http://dx.doi.org/10.3390/ijms21031127.

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Microbial transglutaminase (mTG) is a survival factor for microbes, but yeasts, fungi, and plants also produce transglutaminase. mTG is a cross-linker that is heavily consumed as a protein glue in multiple processed food industries. According to the manufacturers’ claims, microbial transglutaminase and its cross-linked products are safe, i.e., nonallergenic, nonimmunogenic, and nonpathogenic. The regulatory authorities declare it as “generally recognized as safe” for public users. However, scientific observations are accumulating concerning its undesirable effects on human health. Functionally

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Watanabe, Yuko, Kazuho Okuya, Yuki Takada, et al. "Gene disruption of medaka (Oryzias latipes) orthologue for mammalian tissue-type transglutaminase (TG2) causes movement retardation." Journal of Biochemistry 168, no. 3 (2020): 213–22. http://dx.doi.org/10.1093/jb/mvaa038.

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Abstract Transglutaminases are an enzyme family that catalyses protein cross-linking essential for several biological functions. In the previous studies, we characterized the orthologues of the mammalian transglutaminase family in medaka (Oryzias latipes), an established fish model. Among the human isozymes, tissue-type transglutaminase (TG2) has multiple functions that are involved in several biological phenomena. In this study, we established medaka mutants deficient for the orthologue of human TG2 using the CRISPR/Cas9 and transcription activator-like effector nucleases systems. Although ap

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Xavier, Janifer Raj, K. V. Ramana, and R. K. Sharma. "Screening and statistical optimization of media ingredients for production of microbial transglutaminase." Defence Life Science Journal 2, no. 2 (2017): 216. http://dx.doi.org/10.14429/dlsj.2.11369.

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<p>Transglutaminase is a calcium dependent enzyme that catalyses acyl transfer reactions between primary amino groups and protein bound glutamine residues. Eighteen bacterial and twenty eight actinomycetes were screened for the presence of transglutaminase. Among the microbial cultures screened <em>Streptomyces</em> sp. D1, showed maximum transglutaminase activity. In this study characterization of transglutaminase and its application to modifying the properties of panner (Indian cottage cheese) in the form of cross linking was investigated. Optimum temperature and pH for enz

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Dissertations / Theses on the topic "Transglutaminase"

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Guyot, Christopher [Verfasser]. "Transglutaminase-induzierte und Transglutaminase-unterstützte Gele aus Milchproteinen / Christopher Guyot." München : Verlag Dr. Hut, 2013. http://d-nb.info/1045988979/34.

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GIORDANO, DEBORAH. "Transglutaminase, nutrition and human health." Doctoral thesis, Università degli Studi di Foggia, 2019. http://hdl.handle.net/11369/382619.

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Conoscenze preesistenti: Le transglutaminasi (TGase) sono una classe di enzimi ampiamente diffusa tra gli organismi procarioti ed eucarioti. Gli enzimi di questa famiglia catalizzano modifiche post-traduzionali in molte proteine attraverso reazioni di trasferimento dell’acile, reazioni di deaminazione e di crosslinking (polimerizzazione) tra residui peptidici di lisina (accettore di acile) e glutammina (donatore di acile) intra- o inter-catena proteica. A causa della sua facilità di espressione e di purificazione, l’unica TGase ampiamente usata per le applicazioni industriali è la TGase microb

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Bagagli, Marcela Pavan 1981. "Produção de transglutaminase de Streptomyces sp.CBMAI-837 utlizando resíduos ou subprodutos agroindustriais e aplicação em farinha de trigo." [s.n.], 2014. http://repositorio.unicamp.br/jspui/handle/REPOSIP/254358.

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Orientador: Hélia Harumi Sato<br>Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos<br>Made available in DSpace on 2018-08-24T06:55:18Z (GMT). No. of bitstreams: 1 Bagagli_MarcelaPavan_D.pdf: 5889679 bytes, checksum: 9bd456830fa35028a89bffb19885f07d (MD5) Previous issue date: 2014<br>Resumo: A transglutaminase catalisa a formação de ligações cruzadas entre grupos ?-amino de resíduos de lisina e o grupo ?-carboxiamida de resíduos de glutamina de proteínas. Esta enzima pode ser usada para unir diferentes proteínas e melhorar suas propriedades funcionais.

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Johnson, Timothy Scott. "Transglutaminase apoptosis and tumour progression." Thesis, Nottingham Trent University, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.283035.

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Carvalho, Priscila Hoffmann 1983. "Conversão de sacarose em isomaltulose e trealulose utilizando-se células de Serratia plymuthica ATCC 15928 livres e imobilizadas em diferentes matrizes com adição de transglutaminase." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/254359.

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Orientador: Hélia Harumi Sato<br>Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos<br>Made available in DSpace on 2018-08-23T16:00:04Z (GMT). No. of bitstreams: 1 Carvalho_PriscilaHoffmann_D.pdf: 4102242 bytes, checksum: 1496382da70a395d87d5c8536317d42d (MD5) Previous issue date: 2013<br>Resumo: A isomaltulose e a trealulose são dissacarídeos isômeros estruturais, que podem ser obtidos a partir da sacarose utilizando-se glicosiltransferase bacteriana. Esses dissacarídeos são considerados açúcares alternativos de grande potencial para uso nas indústria

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West, Natasha. "Nanocomposite immunosensor for anti-transglutaminase antibody." Thesis, University of the Western Cape, 2009. http://etd.uwc.ac.za/index.php?module=etd&action=viewtitle&id=gen8Srv25Nme4_6426_1298354109.

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<p>Coeliac disease (CD) is a gluten intolerance condition that results in the flattening of the villi, which line the bowel. It is the most common cause of malabsorption of food nutrients. This inability to absorb sufficient levels of nutrients causes many of the common symptoms experienced by CD patients. Some of the symptoms, which lead to an increase in mortality rate, include chronic diarrhea, fatigue, iron-deficient anemia and osteoporosis. People with CD have higher than normal levels of certain antibodies in their blood. Thus, the concentration of anti-transglutaminase antibody (anti-tT

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Gaudrey, Claire Anne. "Tissue transglutaminase : a new secretory protein." Thesis, Nottingham Trent University, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.245102.

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Knight, C. Rosamund L. "Transglutaminase activity, tumour growth and metastasis." Thesis, Nottingham Trent University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.278115.

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Sulic, Ana-marija. "Identification of tissue transglutaminase protein network." Doctoral thesis, Università degli studi di Trieste, 2011. http://hdl.handle.net/10077/4484.

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2009/2010<br>Tissue transglutaminase (TG2) is a multifunctional enyzme involved in cell growth and differentiantion, receptor mediated endocytosis, cell adhesion and morphology, stabilization of extracellular matrix, membrane trafficking and structure/function, signal transduction, regulation of cytoskeleton and apoptosis. Multiple lines of evidence suggest an involvement of TG2 autoimmune diseases, cancer and in neurodegenerative diseases, including Alzheimer's disease, progressive supranuclear palsy, Huntington's disease and Parkinson's disease. In all of the neurodegenerative diseases exa

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Melo, Ricardo Rodrigues de 1985. "Produção e caracterização bioquímica de uma nova transglutaminase microbiana = Production and biochemical characterization of a new microbial transglutaminase." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/254360.

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Orientador: Hélia Harumi Sato<br>Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos<br>Made available in DSpace on 2018-08-22T23:52:05Z (GMT). No. of bitstreams: 1 Melo_RicardoRodriguesde_M.pdf: 1621799 bytes, checksum: 14182717e9ba5de8c1d5014f330c1b6c (MD5) Previous issue date: 2013<br>Resumo: Transglutaminase é uma enzima capaz de catalisar a formação de ligações cruzadas intra- e intermoleculares entre proteínas, peptídeos e aminas primárias por meio de ligações covalentes entre resíduos de lisina e glutamina. Desta forma, transglutaminase pod

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Books on the topic "Transglutaminase"

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Windle, J. M. The role of transglutaminase in tumour growth and metastasis. University of Birmingham, 1985.

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Lantto, R. Protein cross-linking with oxidative enzymes and transglutaminase: Effects in meat protein systems. VTT Technical Research Centre of Finland, 2007.

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Hitomi, Kiyotaka, Soichi Kojima, and Laszlo Fesus, eds. Transglutaminases. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55825-5.

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Castellano, Immacolata. Gamma-glutamyl transpeptidases: Structure and function. Springer, 2013.

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Transglutaminase. Springer, 2012.

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Najjar, V. A., and Laszlo Lorand. Transglutaminase. Springer London, Limited, 2012.

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Najjar, V. A. Transglutaminase. Springer, 2011.

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Zhang, Yi, and Benjamin K. Simpson. Transglutaminase: Fundamentals and Applications. Elsevier Science & Technology Books, 2024.

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Saber, Yasmin. Multimerisierung von Thyreoglobulin: Identifizierung einer Transglutaminase für die kovalente Quervernetzung von Thyreoglobulin. 1997.

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10

Geldmann, Hermann. Plasmatische Protransglutaminase, Faktor XIII und thrombinaktivierte Transglutaminase (Faktor XIIIa) regulieren Gemeinam die Fibrinvernetzung und - Stabilisierung. 1988.

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Book chapters on the topic "Transglutaminase"

1

Cooper, A. J. L., and S. Y. Kim. "Transglutaminase." In Handbook of Neurochemistry and Molecular Neurobiology. Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-30379-6_7.

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Keillor, Jeffrey W. "Inhibition of Transglutaminase." In Transglutaminases. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55825-5_16.

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Shibata, Toshio, and Shun-ichiro Kawabata. "Transglutaminase in Invertebrates." In Transglutaminases. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55825-5_5.

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Mehta, Kapil. "Transglutaminase-2." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_5922-3.

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Mehta, Kapil. "Transglutaminase-2." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_5922.

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Mehta, Kapil. "Transglutaminase-2." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5922.

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Ichinose, Akitada. "Extracellular Transglutaminase: Factor XIII." In Transglutaminases. KARGER, 2005. http://dx.doi.org/10.1159/000084241.

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Kim, Soo-Youl. "Transglutaminase 2-Mediated Gene Regulation." In Transglutaminases. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55825-5_7.

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Iversen, Rasmus, and Ludvig M. Sollid. "Transglutaminase 2 and Celiac Disease." In Transglutaminases. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55825-5_9.

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Singh, Ugra S., and Jing Pan. "Transglutaminase and Cell-Survival Signaling." In Transglutaminases. KARGER, 2005. http://dx.doi.org/10.1159/000084234.

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Conference papers on the topic "Transglutaminase"

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Clare, D., G. Gharst, and T. Sanders. "Transglutaminase Polymerization of Peanut Proteins." In 13th World Congress of Food Science & Technology. EDP Sciences, 2006. http://dx.doi.org/10.1051/iufost:20060479.

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Kaartinen, Mari T., Sherif El-Maadawy, Niina H. Rasanen, Pekka H. Maenpaa, Janet Moradian-Oldak, and Marc D. McKee. "OSTEOPONTIN AS A SUBSTRATE FOR TRANSGLUTAMINASE." In 3rd International Conference on Osteopontin and SIBLING (Small Integrin-Binding Ligand, N-linked Glycoprotein) Proteins, 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.256.

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Pan, Chia-Pin, Jeanne P. Haushalter, Khalid Amin, Zishan Haroon, and Gregory W. Faris. "Fluorescent Tissue Transglutaminase Substrates for Tumor Boundary Imaging." In Frontiers in Optics. OSA, 2007. http://dx.doi.org/10.1364/fio.2007.jwc22.

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Olsen, KC, RE Sapinoro, AJ Filiano, GV Johnson, RP Phipps, and PJ Sime. "Tissue Transglutaminase Is a Novel Regulator of Pulmonary Fibrogenesis." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2699.

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Schulze-Krebs, Anja, Fabio Canneva, Rebecca Schnepf, et al. "A20 A role for transglutaminase 6 in hd pathology." In EHDN 2018 Plenary Meeting, Vienna, Austria, Programme and Abstracts. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/jnnp-2018-ehdn.19.

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Rossane Santana Costa de Souza, Déborah, Bruno Henrique Fermino Goulart, Eric Campos Abreu Fernandes, Túlio Rolim Barretto, and Thiago Andrade Marques. "Transglutaminase: Obtenção, Caracterização e Aplicações na Indústria de Alimentos." In Simpósio de Bioquímica e Biotecnologia. Galoa, 2017. http://dx.doi.org/10.17648/simbbtec-2017-80843.

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Klishchova, Zhanna, Viktoriia Petrashenko, Yurii Ataman, Jarmila Pekarcikova, Tetiana Dereka, and Sergiy Kyrylenko. "Transglutaminase in food adulteration and perspectives of sustainable development." In V International Conference on European Dimensions of Sustainablе Development. National University of Food Technologies, 2023. https://doi.org/10.24263/edsd-2023-5-33.

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Li, Yonghui, Shan Hong, and Yanting Shen. "Enhancing pea protein functionalities through "green" modifications for food applications." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/dpor5716.

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Pea protein is receiving significant interest. Modified pea proteins may be used as healthy and more functional ingredients in food products. This study aimed to enhance pea protein functional properties through neoglycosylation with guar gum or gum arabic and/or enzymatic modification with transglutaminase or protein glutaminase, understand the physicochemical properties of the modified proteins, and evaluate their applications in mayonnaise-like dressings as egg replacers and in beef patties as functional extenders. The proteins crosslinked with transglutaminase showed significantly improved

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Gharst, G., D. Clare, J. Davis, and T. Sanders. "Transglutaminase Effects on the Rheological Characteristics of Peanut Flour Dispersions." In 13th World Congress of Food Science & Technology. EDP Sciences, 2006. http://dx.doi.org/10.1051/iufost:20060475.

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Yang, Chunhua, Yanguo Shi, Ying Liu, Tingting Fan, Yifang Zhang, and Chunlin Hu. "Study on the Aggregation of Transglutaminase on Soybean Protein Hydrolysates." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5514979.

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Reports on the topic "Transglutaminase"

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Mehta, Kapil. Significance of Transglutaminase Expression in Multi-Drug Resistant Tumor Cells. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada413804.

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Haroon, Zishan, and C. Greenberg. Role of Tissue Transglutaminases in Breast Cancer. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada394748.

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Haroon, Zishan A. Role of Tissue Transglutaminases in Breast Cancer. Defense Technical Information Center, 1998. http://dx.doi.org/10.21236/ada358448.

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Zishan, Haroon. Role of Tissue Transglutaminases in Breast Cancer. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada376466.

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