Relevant bibliographies by topics / Enzymatic modifications

Academic literature on the topic 'Enzymatic modifications'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Enzymatic modifications"

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Bensaad, Dhiya Eddine, Mohammed Saleh, Khalid Ismail, and Youngseung Lee. "Recent Advances in Physical, Enzymatic, and Genetic Modifications of Starches." Jordan Journal of Agricultural Sciences 18, no. 3 (September 1, 2022): 245–58. http://dx.doi.org/10.35516/jjas.v18i3.474.

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The current review presents the potential physical modification devised into thermal which includes pre-gelatinization and hydrothermal processing (i.e., annealing (ANN) and heat-moisture treatment (HMT)) and nonthermal modifications (i.e., high-pressure processing (HPP), micronization, ultrasonication, and pulsed electric field (PEF)). Rather than physical modification; enzymatic modification by single enzyme treatment, debranching enzymes, and multienzyme synergetic treatment was discussed. Genetic modification was also discussed as a potential starch modification for better utilization of starch.
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Das, Rakha Hari, Rajesh Ahirwar, Saroj Kumar, and Pradip Nahar. "Microwave-mediated enzymatic modifications of DNA." Analytical Biochemistry 471 (February 2015): 26–28. http://dx.doi.org/10.1016/j.ab.2014.11.003.

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Bensaad, Dhiya Eddine, Mohammed Saleh, Khalid Ismail, Youngseung Lee, and George Ondier. "Chemical Modifications of Starch; A Prospective for Sweet Potato Starch." Jordan Journal of Agricultural Sciences 18, no. 4 (December 1, 2022): 293–308. http://dx.doi.org/10.35516/jjas.v18i4.802.

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The current review presents the potential chemical modifications and applications of sweet potato starch in food and non-food industries. Native starch in general and particularly sweet potato starch characteristics have several functional features and applications in biomedicine as well as in the food industry. Modified starch is expected to enhance such characteristics as discussed in this review. For instance, due to the polymeric and branching nature of starch; the starch is usually less soluble, absorbs less water and oil, and shows a strong ability to bind to iodine. Also, native starches have significantly lower digestibility values under enzymatic treatment. Starch modifications, therefore are designed to enhance one or more of the above-mentioned limitations; thereby, modification of starch can alter the physicochemical characteristics of the native starch to improve its functional characteristic. Starches can be modified using physical methods (annealing, heat moisture treatment, pre-gelatinization, and other non-thermal processes), chemical methods (etherification, acetylation, acid modification, cationic linking, esterification, cross-linking, and oxidation), enzymatic modification methods, genetic alteration process or combination of them.
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Pourmohammadi, Kiana, and Elahe Abedi. "Enzymatic modifications of gluten protein: Oxidative enzymes." Food Chemistry 356 (September 2021): 129679. http://dx.doi.org/10.1016/j.foodchem.2021.129679.

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Kondo, Shinichi, and Kunimoto Hotta. "Semisynthetic aminoglycoside antibiotics: Development and enzymatic modifications." Journal of Infection and Chemotherapy 5, no. 1 (1999): 1–9. http://dx.doi.org/10.1007/s101560050001.

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Yamamoto, Yasuhiko, and Hiroshi Yamamoto. "Enzymatic and non‐enzymatic post‐translational modifications linking diabetes and heart disease." Journal of Diabetes Investigation 6, no. 1 (June 24, 2014): 16–17. http://dx.doi.org/10.1111/jdi.12248.

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Treffon, Patrick, and Elizabeth Vierling. "Focus on Nitric Oxide Homeostasis: Direct and Indirect Enzymatic Regulation of Protein Denitrosation Reactions in Plants." Antioxidants 11, no. 7 (July 21, 2022): 1411. http://dx.doi.org/10.3390/antiox11071411.

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Protein cysteines (Cys) undergo a multitude of different reactive oxygen species (ROS), reactive sulfur species (RSS), and/or reactive nitrogen species (RNS)-derived modifications. S-nitrosation (also referred to as nitrosylation), the addition of a nitric oxide (NO) group to reactive Cys thiols, can alter protein stability and activity and can result in changes of protein subcellular localization. Although it is clear that this nitrosative posttranslational modification (PTM) regulates multiple signal transduction pathways in plants, the enzymatic systems that catalyze the reverse S-denitrosation reaction are poorly understood. This review provides an overview of the biochemistry and regulation of nitro-oxidative modifications of protein Cys residues with a focus on NO production and S-nitrosation. In addition, the importance and recent advances in defining enzymatic systems proposed to be involved in regulating S-denitrosation are addressed, specifically cytosolic thioredoxins (TRX) and the newly identified aldo-keto reductases (AKR).
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Romero, Elvira, Bethan S. Jones, Bethany N. Hogg, Arnau Rué Casamajo, Martin A. Hayes, Sabine L. Flitsch, Nicholas J. Turner, and Christian Schnepel. "Enzymatic Late‐Stage Modifications: Better Late Than Never." Angewandte Chemie International Edition 60, no. 31 (March 8, 2021): 16824–55. http://dx.doi.org/10.1002/anie.202014931.

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Castellani, Oscar F., E. Nora Martínez, and M. Cristina Añón. "Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis." Journal of Agricultural and Food Chemistry 48, no. 11 (November 2000): 5624–29. http://dx.doi.org/10.1021/jf000624o.

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Jung, Guenther. "Smart peptide libraries are accessible via enzymatic modifications." Letters in Peptide Science 8, no. 3-5 (May 2001): 259–65. http://dx.doi.org/10.1007/bf02446526.

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Dissertations / Theses on the topic "Enzymatic modifications"

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Guedes, Sofia de Morais Correia Pereira. "Study of oxidation and non-enzymatic glycosylation posttranslational modifications using a proteomic approach." Doctoral thesis, Uniiversidade de Aveiro, 2011. http://hdl.handle.net/10773/7034.

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Doutoramento em Bioquímica
A glicosilação não-enzimática e o stress oxidativo representam dois processos importantes visto desempenharem um papel importante no que respeita às complicações de vários processos patofisiológicos. No presente, a associação entre a glicosilação não-enzimática e a oxidação de proteínas é reconhecida como sendo um dos principais responsáveis pela acumulação de proteínas não-funcionais que, por sua vez, promove uma contínua sensibilização para um aumento do stress oxidativo ao nível celular. Embora esteja disponível bastante informação no que respeita aos dois processos e suas consequências ao nível estrutural e funcional, permanecem questões por esclarecer acerca do que se desenvolve ao nível molecular. Com o objectivo de contribuir para uma melhor compreensão da relação entre a glicosilação não-enzimática e a oxidação, proteínas modelo (albumina, insulina e histonas H2B e H1) foram submetidas a sistemas in vitro de glicosilação não-enzimática e oxidação em condições controladas e durante um período de tempo específico. A identificação dos locais de glicosilação e oxidação foi realizada através de uma abordagem proteómica, na qual após digestão enzimática se procedeu à análise por cromatografia líquida acoplada a espectrometria de massa tandem (MALDI-TOF/TOF). Esta abordagem permitiu a obtenção de elevadas taxas de cobertura das sequências proteicas, permitindo a identificação dos locais preferenciais de glicosilação e oxidação nas diferentes proteínas estudadas. Como esperado, os resíduos de lisina foram os preferencialmente glicosilados. No que respeita à oxidação, além das modificações envolvendo hidroxilações e adições de oxigénio, foram identificadas deamidações, carbamilações e conversões oxidativas específicas de vários aminoácidos. No geral, os resíduos mais afectados pela oxidação foram os resíduos de cisteína, metionina, triptofano, tirosina, prolina, lisina e fenilalanina. Ao longo do período de tempo estudado, os resultados indicaram que a oxidação teve início em zonas expostas da proteína e/ou localizadas na vizinhança de resíduos de cisteína e metionina, ao invés de exibir um comportamente aleatório, ocorrendo de uma forma nãolinear por sua vez dependente da estabilidade conformacional da proteína. O estudo ao longo do tempo mostrou igualmente que, no caso das proteínas préglicosiladas, a oxidação das mesmas ocorreu de forma mais rápida e acentuada, sugerindo que as alterações estruturais induzidas pela glicosilação promovem um estado pro-oxidativo. No caso das proteínas pré-glicosiladas e oxidadas, foi identificado um maior número de modificações oxidativas assim como de resíduos modificados na vizinhança de resíduos glicosilados. Com esta abordagem é realizada uma importante contribuição na investigação das consequências do dano ‘glico-oxidativo’ em proteínas ao nível molecular através da combinação da espectrometria de massa e da bioinformática.
Glycation and oxidative stress are two important processes known to play a key role in complications of many pathophysiological processes. It is nowadays acknowledged the association between glycation and oxidation events as a major responsible for the accumulation of non-functional damaged proteins that in turn promote continuous sensitization to further oxidative stress at the cellular level. Despite the large amount of information concerning both events and their consequences at structural and functional levels, questions remain to answer on what happens at the protein molecular level. With the aim of contributing to better understand the interrelationship between glycation and oxidation, model proteins (BSA, insulin and histones H2B and H1) were submitted to in vitro systems of glycation and oxidation under controlled conditions and through a specific period of time. Identification of glycation and oxidation sites was performed through a proteomics approach. Protein samples were enzimatically digested and further analyzed by nano-liquid chromatography coupled to MALDI-TOF/TOF mass spectrometry. This approach allowed obtaining high protein coverage rates, enabling the identification of the most susceptible sites of glycation and oxidation in the different studied proteins. As expected, lysine residues were preferentially glycated and with respect to oxidation, besides protein hydroxyl derivatives and oxygen additions, modifications such as deamidations, carbamylations and specific amino acid oxidative conversions were detected. In general, the main affected amino acids by oxidative damage were cysteine, methionine, tryptophan, tyrosine, proline, lysine and phenylalanine. The time-course study of the oxidative damage indicated the oxidative attack, rather than occurring randomly, initiates at surface-exposed regions and/or near cysteine and methionine residues and occurs in a non-linear way depending on the conformational stability of the protein. Time-course analysis also showed a more pronounced and earlier occurrence of the oxidative damage in the case of preglycated proteins, suggesting that structural changes caused by glycation induce a pro-oxidant state. This increased oxidative damage included not only a greater number of oxidative modifications, but also of oxidized residues, occurring in the vicinity of the glycated residues. Through this kind of approach, an important contribution is made in the investigation of the consequences of protein ‘glycoxidative’ damage at a molecular level through the profit combination of mass spectrometry and bioinformatics.
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Baron, Kim L. "Enzymatic and chemical modifications of erythrocyte surface antigens to identify Plasmodium falciparum merozoite binding sites." Diss., University of Pretoria, 2014. http://hdl.handle.net/2263/46043.

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Malaria is a disease caused by the protozoan parasite Plasmodium where the species that causes the most severe form of malaria in humans is known as Plasmodium falciparum. At least 40% of the global population is at risk of contracting malaria with 627 000 people dying as a result of this disease in 2012. Approximately 90% of all malaria deaths occur in sub-Saharan Africa, where approximately every 30 seconds a young child dies, making malaria the leading cause of death in children under the age of five years old. The malaria parasite has a complex life cycle utilising both invertebrate and vertebrate hosts across sexual and asexual stages. The erythrocyte invasion stage of the life cycle in the human whereby the invasive merozoite form of the parasite enters the erythrocyte is a central and essential step, and it is during this stage that the clinical symptoms of malaria manifest themselves. Merozoites invade erythrocytes utilising multiple, highly specific receptor-ligand interactions in a series of co-ordinated events. The aim of this study was to better understand the interactions occurring between the merozoite and erythrocyte during invasion by using modern, cutting-edge proteomic techniques. This was done in the hope of laying the foundation for the discovery of new key therapeutic targets for antimalarial drug and vaccine-based strategies, as there is currently no commercially available antimalarial vaccine and no drug to which the parasite has not at least started showing resistance. In this study healthy human erythrocytes were treated separately with different protein-altering enzymes and chemicals being trypsin, the potent oxidant sodium periodate (NaIO4), the amine cross-linker tris(2-chloroethyl)amine hydrochloride (TCEA) and the thiol cross-linker 1,11-bis(maleimido)triethylene glycol (BM(PEG)3). The resulting erythrocyte protein alterations were visualised as protein band differences on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE), where treated and untreated control erythrocyte ghost protein fingerprints were visually compared to one another. The protein bands showing differences between treated and control samples were in-gel digested using trypsin then sequenced by liquid chromatography tandem mass spectrometry (LC-MS/MS) and identified using proteomics-based software. In this way, the erythrocyte proteins altered by each enzyme/chemical treatment were identified. Malaria invasion assays were performed where each treatment group of erythrocytes as well as the control erythrocytes were incubated separately with schizont stage malaria parasites for the duration of one complete life cycle. Using fluorescent staining and flow cytometry, the invasion inhibition efficiency for each treatment group was evaluated. By utilising these methods, the identification and the relative importance of the erythrocyte proteins involved in the invasion process were determined. Protein fingerprints of control and treated erythrocyte ghosts were visualised and optimised on SDS PAGE where induced protein band differences were successfully identified by LC-MS/MS. It was found that each treatment altered erythrocyte proteins with changes found in Band 3, actin, phosphoglycerate kinase 1, spectrin alpha, spectrin beta, ankyrin, haemoglobin, Bands 4.1 and 4.2, glycophorin A and stomatin. The invasion assays revealed that TCEA inhibited invasion to the greatest extent as compared to the other treatments, followed by BM(PEG)3 and trypsin. Sodium periodate-treated erythrocytes could not be assessed using the invasion assay due to auto-haemolysis. Band 3, glycophorin A, Band 4.1 and stomatin appear to be of higher relative importance in the invasion process as compared to the other altered erythrocyte proteins. These results confirmed the known roles of spectrin alpha, spectrin beta, glycophorin A, Band 3 and Band 4.1 in invasion, and suggested that ankyrin, Band 4.2 and stomatin may also be involved. This study highlighted the potential that modern, cutting-edge proteomic techniques provide when applied to previous comparative studies found in older literature, as previously unidentified proteins that can be involved in invasion were revealed. These results can be used as a foundation in future studies in order to identify new key targets for the development of new antimalarial drug- and vaccine-based strategies, with the hope of preventing the suffering of the millions of malaria-inflicted people worldwide, and ultimately eradicating this deadly disease.
Dissertation (MSc)--University of Pretoria, 2014.
tm2015
Pharmacology
MSc
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Simiand, Cécile. "Modifications régio- et stéréosélectives du saccharose." Grenoble 1, 1993. http://www.theses.fr/1993GRE10180.

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Les dextrane-saccharases utilisent le saccharose comme glucosyle donneur pour la biosynthese de dextranes. Des saccharoses modifies ont ete synthetises puis testes comme analogues de substrat de ces enzymes. Le 3-oxo-saccharose, obtenu par biooxydation du saccharose, a ete utilise comme compose precurseur pour les modifications en c-3. Les 3-oximino, 3-amino et 3-thio-saccharoses ont ete obtenus avec de bons rendements. La strategie developpee pour les modifications en position c-4 a permis d'obtenir, de facon stereoselective, les 4-amino, 4-thio et 4-fluoro-saccharoses. Des tests enzymatiques en presence de dextrane-saccharases ont mis en evidence le caractere inhibiteur des amino et thio-saccharoses
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Kutacova, Pavla. "Enzymatic modification of kenaf pulp." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ33973.pdf.

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Mansfield, Shawn Denton. "Enzymatic modification of Douglas-fir pulp." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/NQ27197.pdf.

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Dalponte, Luca. "Chemo-enzymatic modification of cyclic peptides." Thesis, University of Aberdeen, 2018. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=239393.

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簫乃志 and Nai-chi Siu. "Enzymatic modification of oat globulin by microbial transglutaminase." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2001. http://hub.hku.hk/bib/B31225147.

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Siu, Nai-chi. "Enzymatic modification of oat globulin by microbial transglutaminase." Hong Kong : University of Hong Kong, 2001. http://sunzi.lib.hku.hk/hkuto/record.jsp?B23234507.

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Kriek, Marco. "Enzymatic synthesis of complex carbohydrates : approaches to the enzymatic synthesis and chemical modification of oligosaccharides." Thesis, University of Reading, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342146.

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Chandra, Richard P. "Chemo-enzymatic modification of high-kappa kraft pulps with laccase." Diss., Available online, Georgia Institute of Technology, 2005, 2003. http://etd.gatech.edu/theses/available/ipstetd-1011/.

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Books on the topic "Enzymatic modifications"

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Gahruie, Hadi Hashemi, Mohammad Hadi Eskandari, Amin Mousavi Khaneghah, and Fatemeh Ghiasi, eds. Physicochemical and Enzymatic Modification of Gums. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-87996-9.

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Petersson, E. James. Synthetic and Enzymatic Modifications of the Peptide Backbone. Academic Press, 2021.

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Synthetic and Enzymatic Modifications of the Peptide Backbone. Elsevier, 2021. http://dx.doi.org/10.1016/s0076-6879(21)x0012-2.

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Petersson, E. James. Synthetic and Enzymatic Modifications of the Peptide Backbone. Elsevier Science & Technology Books, 2021.

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Sadowska-Bartosz, Izabela, and Grzegorz Bartosz. Non-Enzymatic Protein Modifications in Health, Disease and Ageing. Elsevier Science & Technology Books, 2020.

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Sadowska-Bartosz, Izabela, and Grzegorz Bartosz. Non-Enzymatic Protein Modifications in Health, Disease and Ageing. Elsevier Science & Technology, 2019.

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Aldiab, Dima. LC-ESI-MS-MS analysis of non-enzymatic posttranslational protein modifications. 2011.

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Aldiab, Dima. LC-ESI-MS-MS analysis of non-enzymatic posttranslational protein modifications. 2011.

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Kutacova, Pavla. Enzymatic modification of Kenaf pulp. 1998.

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Khaneghah, Amin Mousavi, Hadi Hashemi Gahruie, Mohammad Hadi Eskandari, and Fatemeh Ghiasi. Physicochemical and Enzymatic Modification of Gums: Synthesis, Characterization and Application. Springer International Publishing AG, 2021.

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Book chapters on the topic "Enzymatic modifications"

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Moorthy, S. N., M. S. Sajeev, R. P. K. Ambrose, and R. J. Anish. "Starch modifications." In Tropical tuber starches: structural and functional characteristics, 177–213. Wallingford: CABI, 2021. http://dx.doi.org/10.1079/9781786394811.0177.

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Abstract This chapter outlines the modification of tuber starches, the properties of modified starches, and the possible areas of application. The nature of modifications (physical, chemical, enzymatic, dual/triple modifications, graft polymerization) and their influence on the functional properties and structure of cassava, sweet potato, yam, aroid (Colocasia esculenta, Xanthosoma sagittifolium, Amorphophallus paeoniifolius and Arracacia xanthorrhiza) and other starches are described.
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Sharma, Sunny, and Karl-Dieter Entian. "Chemical Modifications of Ribosomal RNA." In Ribosome Biogenesis, 149–66. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2501-9_9.

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AbstractCellular RNAs in all three kingdoms of life are modified with diverse chemical modifications. These chemical modifications expand the topological repertoire of RNAs, and fine-tune their functions. Ribosomal RNA in yeast contains more than 100 chemically modified residues in the functionally crucial and evolutionary conserved regions. The chemical modifications in the rRNA are of three types—methylation of the ribose sugars at the C2-positionAbstract (Nm), isomerization of uridines to pseudouridines (Ψ), and base modifications such as (methylation (mN), acetylation (acN), and aminocarboxypropylation (acpN)). The modifications profile of the yeast rRNA has been recently completed, providing an excellent platform to analyze the function of these modifications in RNA metabolism and in cellular physiology. Remarkably, majority of the rRNA modifications and the enzymatic machineries discovered in yeast are highly conserved in eukaryotes including humans. Mutations in factors involved in rRNA modification are linked to several rare severe human diseases (e.g., X-linked Dyskeratosis congenita, the Bowen–Conradi syndrome and the William–Beuren disease). In this chapter, we summarize all rRNA modifications and the corresponding enzymatic machineries of the budding yeast.
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Siegel, Frank L. "Enzymatic N-Methylation of Calmodulin." In Advances in Post-Translational Modifications of Proteins and Aging, 341–51. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-9042-8_27.

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Ellipilli, Satheesh, and Peixuan Guo. "Synthetic and Enzymatic Methods for RNA Labeling and Modifications." In RNA Nanotechnology and Therapeutics, 25–31. 2nd ed. Boca Raton: CRC Press, 2022. http://dx.doi.org/10.1201/9781003001560-7.

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Kim, Sangduk, Latika P. Chanderkar, Subrata K. Ghosh, Jong-Ok Park, and Woon Ki Paik. "Enzymatic Methylation of Arginine Residue in Myelin Basic Protein." In Advances in Post-Translational Modifications of Proteins and Aging, 327–40. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-9042-8_26.

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Jimenez-Flores, Rafael, and Thomas Richardson. "Effects of Chemical, Genetic and Enzymatic Modifications on Protein Functionality." In Food Biotechnology—1, 87–137. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3411-5_3.

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Roth, William J., Soo Il Chung, Linga Raju, and Aaron Janoff. "Macrophage Transglutaminases: Characterization of Molecular Species and Measurement of Enzymatic Modification by Cigarette Smoke Components." In Advances in Post-Translational Modifications of Proteins and Aging, 161–73. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-9042-8_13.

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Paik, Woon Ki, Kwang Sook Park, Blaise F. Frost, and Sangduk Kim. "Effect of Enzymatic Methylation on the Import of in Vitro Synthesized Apocytochrome C into Mitochondria." In Advances in Post-Translational Modifications of Proteins and Aging, 317–25. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-9042-8_25.

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Legrand, J., Y. Popineau, S. Berot, J. Gueguen, and L. Nouri. "Application of a Torus Reactor to Chemical and Enzymatic Modifications of Plant Proteins." In Plant Proteins from European Crops, 297–302. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-03720-1_50.

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Rieder, Renate, Claudia Höbartner, and Ronald Micura. "Enzymatic Ligation Strategies for the Preparation of Purine Riboswitches with Site-Specific Chemical Modifications." In Methods in Molecular Biology, 15–24. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-558-9_2.

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Conference papers on the topic "Enzymatic modifications"

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Bhatt, Chinmayi. "Demonstrating the viability of implementing phospholipases in enzymatic degumming of rapeseed oil." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/tpag6228.

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The efficacy of phospholipases in degumming has been well-documented in soybean oil as a means to increase yields as well as reduce gum volumes. Rapeseed oil, however, remains relatively poorly explored, despite being the dominant feedstock in other regions for refining. With its higher content of metals, phosphatidic acid, and non-hydratable phospholipids, rapeseed oil is often regarded as a more difficult feedstock, practically speaking, to degum enzymatically. This presentation will describe both the standard process and modifications to this process to make phospholipase-assisted alkaline and physical refining as effective (with regards to cost and yield) on rapeseed oil as it has been shown to be on soybean oil. Data from preliminary lab trials on these alternative methods will be evaluated to demonstrate the large potential of phospholipases in rapeseed oil refineries.
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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 water holding capacity (5.2 - 5.6 g/g protein) compared with the control pea protein isolate (2.8 g/g). The pea proteins conjugated with guar gum showed exceptional emulsifying capacity (EC) and stability (ES) of up to 100% compared with the control protein (EC of 58% and ES of 48%). Some sequentially modified pea proteins, such as transglutaminase crosslinking followed by guar gum conjugation had multiple functional enhancements (water holding, oil holding, emulsifying, and gelation). The functionally enhanced pea proteins had comparable descriptive sensory scores as the control protein. Beef patties containing 2.5-5% of the modified pea protein from sequential deamidation and conjugation demonstrated some advantageous features in terms of higher fat/water retention, cooking yield, and tender texture, which may be preferred by the elderly or some other consumers. The emulsions with the guar gum conjugated protein had significantly increased stability, apparent viscosity, and decreased droplet size, and mayonnaise-like dressing prepared with this protein at higher concentrations (6 and 8%) exhibited significantly better emulsification properties and viscoelasticity, compared with those containing the unmodified protein.
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Yang, Jasmin, Fernanda Furlan Goncalves Dias, and Juliana M. Leite Nobrega De Moura Bell. "Sequential Fractionation as a Tool for Understanding the Physicochemical and Thermal Properties of Aqueous and Enzyme-assisted Aqueous Extracted Black Bean Proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qivq4253.

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Black bean proteins were sequentially extracted and characterized to understand the contribution of different protein classes to the physicochemical and thermal properties of black bean protein extracts produced with commercially-feasible extraction processes (i.e., aqueous extraction process, AEP, and enzyme-assisted aqueous extraction process, EAEP). The Osborne fractionation method was used to produce protein fractions rich in albumins (56%), globulins (22%), prolamins (0.65%), and glutelins (16%). AEP (pH 9.0, 50 °C, 1:10 solids-to-liquid ratio, 60 min) and EAEP (same conditions as AEP, except by the addition of 0.5% (w/w) alkaline protease) enabled the extraction of 75 and 81% of the bean flour protein, respectively. The protein molecular weight distribution showed that the AEP generates a mixture of albumins, globulins, and high-molecular weight glutelins while the EAEP hydrolyzed a majority of the ~42-48 kDa phaseolin into ~26.5 kDa fragments. EAEP proteins exhibited decreased surface hydrophobicity and increased absolute zeta potential values in relation to AEP proteins. The thermal stability of AEP and EAEP proteins decreased compared to that of the albumin- and globulin-rich fractions, likely due to partial denaturation in alkaline extraction conditions. However, the nearly identical thermal transition behavior of the AEP (To = 85.2 °C, Td = 92.0 °C) and EAEP (To = 84.1 °C, Td = 92.3 °C) proteins suggests that enzymatic hydrolysis did not significantly affect the thermal properties of bean proteins. Furthermore, the physicochemical modifications observed when enzymes were used during the extraction resulted in proteins with higher solubility at pH 4.0 (27% for AEP vs. 60% for EAEP). The results of this study demonstrate that aqueous extraction methods are effective in extracting albumins, globulins, and glutelins from black beans. Moreover, the use of commercial enzymes to assist protein extraction is a feasible method to improve bean protein extractability and functionality while retaining their thermal stability.
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Bogojevic, Oliver, Carl Arevang, and Zheng Guo. "Synthesis of complex phospholipid species." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/rlyh7861.

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Phospholipids are essential for the preservation of life on the planet and carry numerous critical roles and functions, including being the main constituents of the cell-membranes in both eukaryotic and prokaryotic cells, providing (more bioavailable) energy, and maintaining chemical and electrical processes in the body. The structural characteristics of phospholipids can vary greatly among species, however, commonly consist of a hydrophilic region (phosphate-containing head-group) and a hydrophobic region (fatty acids, €œtails€), providing the amphiphilic features and unique functions. The countless number of possible configurations enables the continuous synthesis of novel phospholipid species. The synthesis of specific phospholipids, so-called €œdesigner-phospholipids€, is commonly carried out through modifications of more common and easily accessible phospholipid species, catalyzed by the use of either non-specific chemical catalysts or specific enzymes. Enzymatic methods, being most prominent, are often using biphasic reaction systems, allowing for the easy reuse of enzymes and separation of polar compounds, offering more environmentally friendly approaches'. The synthesis of complex phospholipids such as cardiolipins (CLs) and bis(mono/di-acylglycero)phopshates (BMPs/BDPs) have significant value as they carry the unique ability to contain multiple fatty acids, which in turn can be linked to a range of positive health effects. The positive health effects of fish oils (EPA/DHA) are today a hot topic, which in combination with complex phospholipids present great potential for future applications. Additionally, new phospholipid species are continuously under development utilizing completely new synthetic systems with environmentally friendly approaches' in focus. Modern methods centralized on the combinatorial use of ionic liquids and enzymes for the production of novel phospholipids species reduce the use of organic solvents, allowing for the incorporation of fatty acid esters of hydroxy fatty acids (FAHFAs) into phospholipids. The science behind the synthesis of phospholipids is continuously developing for an increased amount of different applications.
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Koentjoro, Maharani Pertiwi, Marisa Fitriana, Isdiantoni, and Endrv Nugroho Prasetyo. "Enzymatic modification of cotton fiber for promising smart medical based material." In 2018 1st International Conference on Bioinformatics, Biotechnology, and Biomedical Engineering (BioMIC). IEEE, 2018. http://dx.doi.org/10.1109/biomic.2018.8610599.

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Pugachenko, I. S., E. I. Nasybullina, O. V. Kosmachevskaya, and A. F. Topunov. "EFFECT OF NITROXYL ON MODIFICATION OF HEMOGLOBIN BY OXIDATION AND GLYCATION." In NOVEL TECHNOLOGIES IN MEDICINE, BIOLOGY, PHARMACOLOGY AND ECOLOGY. Institute of information technology, 2022. http://dx.doi.org/10.47501/978-5-6044060-2-1.215-219.

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Nitroxyl in biological systems can work as a classic antioxidant. It has been shown that ni-troxyl reduces the yield of free radical products in the reaction of hemoglobin with tert-butyl peroxide. Due to this, nitroxyl slows down the formation of non-enzymatic glycation products in the reaction of hemoglobin with methylglyoxal.
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Mao, Xiangzhao. "Efficient Expression of Phospholipase D and Its Application in Enzymatic Modification of Phospholipids." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.207.

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Amat, Albert, and Ronald W. Waynant. "Modification of enzymatic activity following laser irradiation through the light-induced electric field." In Biomedical Optics 2006, edited by Michael R. Hamblin, Ronald W. Waynant, and Juanita Anders. SPIE, 2006. http://dx.doi.org/10.1117/12.647398.

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Culler, Mitchell, Eric Decker, and Ipek Bayram. "Enzymatic modification of lecithin for improved antioxidant activity in combination with tocopherol in emulsions and bulk oil." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/dsey3101.

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Industry attempts to meet consumers' clean label demands by removing synthetic antioxidants (e.g. EDTA) frequently result in deleterious effects on oil quality, causing the formation of toxic oxidation derivatives as well as off-flavors and aromas. Thus, there is an urgent need for novel and natural antioxidant systems. For example, after becoming oxidized, α-tocopherol can be recharged to its active form by phosphatidylethanolamine (PE) for increased efficacy. Unfortunately, plant-based lecithin is mostly phosphatidylcholine (PC), which lacks the amine group necessary to recharge tocopherol. Purified phospholipids are typically too expensive for food products, however enzymatic conversion of PC to PE is more cost effective.The aims of the present study are 1) to determine the optimal reaction conditions for converting high PC lecithin into modified high PE lecithin (MHPEL) and 2) to validate the MHPEL's synergism with tocopherol in delaying lipid oxidation in model emulsion systems at pH 7, and 4, and in bulk oil. High PC lecithin was incubated with phospholipase D from Streptomyces chromofuscus and ethanolamine at varied pH, temperature, and time and then analyzed for compositional changes by HPLC. To assess shelf life, aliquots of 1% o/w emulsions buffered to pH 7 and 4 as well as bulk oil were prepared and stored at 32 and 55°C, respectively. Treatment groups included control, MHPEL, purified PE standard, tocopherol, tocopherol + MHPEL, and tocopherol + purified PE standard. Lipid hydroperoxide formation was measured spectrophotometrically, and hexanal formation was measured using GC headspace analysis. Maximum conversion occurred at pH 9 and 37°C, reaching >73% PE after 4 hours. The combination of MHPEL and tocopherol increased shelf-life by 75% compared to tocopherol alone in o/w emulsions at pH 7, 50% in o/w emulsions at pH 4, and 100% in bulk oil. This approach represents an exciting and clean-label antioxidant system with commercialization potential.
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Tomczyk, Łukasz, Grzegorz Leśnierowski, and Renata Cegielska-Radziejewska. "Physicochemical Evaluation of Preparations Obtained as a Result of Enzymatic Modification of Lysozymes with Pepsin and Trypsin." In Foods 2022. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/foods2022-12924.

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Reports on the topic "Enzymatic modifications"

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Olszewski, Neil, and David Weiss. Role of Serine/Threonine O-GlcNAc Modifications in Signaling Networks. United States Department of Agriculture, September 2010. http://dx.doi.org/10.32747/2010.7696544.bard.

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Significant evidence suggests that serine/threonine-O-linked N-acetyl glucosamine0-(GlcNAc) modifications play a central role in the regulation of plant signaling networks. Forexample, mutations in SPINDLY,) SPY (an O-GlcNAc transferase,) OGT (promote gibberellin GA) (signal transduction and inhibit cytokinin responses. In addition, mutating both Arabidopsis OGTsSEC (and SPY) causes embryo lethality. The long-term goal of this research is to elucidate the mechanism by which Arabidopsis OGTs regulate signaling networks. This project investigated the mechanisms of O-GlcNAc regulation of cytokinin and gibberellin signaling, identified additional processes regulated by this modification and investigated the regulation of SEC activity. Although SPY is a nucleocytoplasmic protein, its site of action and targets were unknown. Severalstudies suggested that SPY acted in the nucleus where it modified nuclear components such as the DELLA proteins. Using chimeric GFP-SPY fused to a nuclear-export signal or to a nuclear-import signal, we showed that cytosolic, but not nuclear SPY, regulated cytokinin and GA signaling. We also obtained evidence suggesting that GA and SPY affect cytokinin signaling via a DELLA-independent pathway. Although SEC and SPY were believed to have overlapping functions, the role of SEC in cytokinin and GA signaling was unclear. The role of SEC in cytokinin and GA responses was investigated by partially suppressing SPY expression in secplants using a synthetic Spymicro RNA miR(SPY). The possible contribution of SEC to the regulation of GA and cytokinin signaling wastest by determining the resistance of the miR spy secplants to the GA biosynthesis inhibitor paclobutrazol and to cytokinin. We found that the transgenic plants were resistant to paclobutrazol and to cytokinin, butonlyata level similar to spy. Moreover, expressing SEC under the 35S promoter in spy mutant did not complement the spy mutation. Therefore, we believe that SEC does not act with SPY to regulate GA or cytokinin responses. The cellular targets of Spy are largely unknown. We identified the transcription factor TCP15 in a two-hybrid screen for SPY-interacting proteins and showed that both TCP15 and its closely homolog TCP14 were O-GlcNAc modified by bacterially-produced SEC. The significance of the interaction between SPY and these TCPs was examined by over-expressing the minwild-type and spy-4plants. Overexpression of TCP14 or TCP15 in wild-type background produced phenotypes typical of plants with increased cytokinin and reduced GA signaling. TCP14 overexpression phenotypes were strongly suppressed in the spy background, suggesting that TCP14 and TCP15 affect cytokinin and GA signaling and that SPY activates them. In agreement with this hypothesis, we created a tcp14tcp15 double mutant and found that it has defects similar to spyplants. In animals, O-GlcNAc modification is proposed to regulate the activity of the nuclear pore. Therefore, after discovering that SEC modified a nucleoporinNUP) (that also interacts with SPY, we performed genetic experiments exploring the relationship between NUPs and SPY nupspy double mutants exhibited phenotypes consistent with SPY and NUPs functioning in common processes and nupseeds were resistant to GA biosynthesis inhibitors. All eukaryotic OGTs have a TPR domain. Deletion studies with bacterially-expressed SEC demonstrated SEC'sTPR domain inhibits SEC enzymatic activity. Since the TPR domain interacts with other proteins, we propose that regulatory proteins regulate OGT activity by binding and modulating the inhibitory activity of the TPR domain.
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