Base de dados : MEDLINE
Pesquisa : D12.776.053 [Categoria DeCS]
Referências encontradas : 781 [refinar]
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[PMID]:29385175
[Au] Autor:Firdaus-Raih M; Hashim NHF; Bharudin I; Abu Bakar MF; Huang KK; Alias H; Lee BKB; Mat Isa MN; Mat-Sharani S; Sulaiman S; Tay LJ; Zolkefli R; Muhammad Noor Y; Law DSN; Abdul Rahman SH; Md-Illias R; Abu Bakar FD; Najimudin N; Abdul Murad AM; Mahadi NM
[Ad] Endereço:School of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi, Selangor, Malaysia.
[Ti] Título:The Glaciozyma antarctica genome reveals an array of systems that provide sustained responses towards temperature variations in a persistently cold habitat.
[So] Source:PLoS One;13(1):e0189947, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extremely low temperatures present various challenges to life that include ice formation and effects on metabolic capacity. Psyhcrophilic microorganisms typically have an array of mechanisms to enable survival in cold temperatures. In this study, we sequenced and analysed the genome of a psychrophilic yeast isolated in the Antarctic region, Glaciozyma antarctica. The genome annotation identified 7857 protein coding sequences. From the genome sequence analysis we were able to identify genes that encoded for proteins known to be associated with cold survival, in addition to annotating genes that are unique to G. antarctica. For genes that are known to be involved in cold adaptation such as anti-freeze proteins (AFPs), our gene expression analysis revealed that they were differentially transcribed over time and in response to different temperatures. This indicated the presence of an array of adaptation systems that can respond to a changing but persistent cold environment. We were also able to validate the activity of all the AFPs annotated where the recombinant AFPs demonstrated anti-freeze capacity. This work is an important foundation for further collective exploration into psychrophilic microbiology where among other potential, the genes unique to this species may represent a pool of novel mechanisms for cold survival.
[Mh] Termos MeSH primário: Adaptação Fisiológica/genética
Basidiomycota/fisiologia
Temperatura Baixa
Ecossistema
Genoma Fúngico
[Mh] Termos MeSH secundário: Regiões Antárticas
Proteínas Anticongelantes/genética
Basidiomycota/genética
Íntrons
RNA Nucleolar Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (RNA, Small Nucleolar)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189947


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[PMID]:28691252
[Au] Autor:Stevens CA; Semrau J; Chiriac D; Litschko M; Campbell RL; Langelaan DN; Smith SP; Davies PL; Allingham JS
[Ad] Endereço:Protein Function Discovery Group and the Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, K7L 3N6, Canada.
[Ti] Título:Peptide backbone circularization enhances antifreeze protein thermostability.
[So] Source:Protein Sci;26(10):1932-1941, 2017 Oct.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Antifreeze proteins (AFPs) are a class of ice-binding proteins that promote survival of a variety of cold-adapted organisms by decreasing the freezing temperature of bodily fluids. A growing number of biomedical, agricultural, and commercial products, such as organs, foods, and industrial fluids, have benefited from the ability of AFPs to control ice crystal growth and prevent ice recrystallization at subzero temperatures. One limitation of AFP use in these latter contexts is their tendency to denature and irreversibly lose activity at the elevated temperatures of certain industrial processing or large-scale AFP production. Using the small, thermolabile type III AFP as a model system, we demonstrate that AFP thermostability is dramatically enhanced via split intein-mediated N- and C-terminal end ligation. To engineer this circular protein, computational modeling and molecular dynamics simulations were applied to identify an extein sequence that would fill the 20-Å gap separating the free ends of the AFP, yet impose little impact on the structure and entropic properties of its ice-binding surface. The top candidate was then expressed in bacteria, and the circularized protein was isolated from the intein domains by ice-affinity purification. This circularized AFP induced bipyramidal ice crystals during ice growth in the hysteresis gap and retained 40% of this activity even after incubation at 100°C for 30 min. NMR analysis implicated enhanced thermostability or refolding capacity of this protein compared to the noncyclized wild-type AFP. These studies support protein backbone circularization as a means to expand the thermostability and practical applications of AFPs.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/química
Proteínas Anticongelantes/metabolismo
Estabilidade Proteica
[Mh] Termos MeSH secundário: Proteínas Anticongelantes/genética
Sítios de Ligação/genética
Temperatura Alta
Gelo
Simulação de Dinâmica Molecular
Ressonância Magnética Nuclear Biomolecular
Conformação Proteica
Engenharia de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Ice)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3228


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[PMID]:28534053
[Au] Autor:Tomalty HE; Hamilton EF; Hamilton A; Kukal O; Allen T; Walker VK
[Ad] Endereço:Department of Biology, Queen's University, Kingston, Ontario, Canada.
[Ti] Título:Kidney preservation at subzero temperatures using a novel storage solution and insect ice-binding proteins.
[So] Source:Cryo Letters;38(2):100-107, 2017 Mar/Apr.
[Is] ISSN:0143-2044
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Contemporary kidney preservation methods involve storing at 4 degree C up to 24 h prior to transplantation. By decreasing the storage temperature to below 0 degree C, we hypothesized that the safe storage time could be significantly lengthened. OBJECTIVE: The efficacy of a proprietary CryoStasis (CrS) storage solution for the subzero preservation of kidneys was tested, with or without addition of a hyperactive insect antifreeze protein (TmAFP). MATERIALS AND METHODS: Rat kidneys were stored in either University of Wisconsin (UW) solution (4 degree C, 24 h), CrS (-2 degree C, 48 h), or CrS with 61.5 µM TmAFP (-4.4 degree C, 72 h). Following storage, viability was assessed with MTT reduction assays and live vs. dead cell (FDA/PI) staining. Markers of ischemic damage were analyzed using fluormetric substrates for caspase-3 and calpain activity. RESULTS: Kidneys stored in CrS for 48 h and CrS with TmAFP for 72 h displayed similar levels of enzymatic activity compared to 24 h UW controls. CONCLUSION: This methodology shows promise to prolong the safe storage time of kidneys and offers the potential of increased organ availability for renal transplants.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/farmacologia
Criopreservação/métodos
Proteínas de Insetos/farmacologia
Rim
Preservação de Órgãos/métodos
[Mh] Termos MeSH secundário: Animais
Calpaína/metabolismo
Caspase 3/metabolismo
Temperatura Baixa
Glutationa/metabolismo
Rim/efeitos dos fármacos
Rim/metabolismo
Transplante de Rim/métodos
Masculino
Soluções para Preservação de Órgãos/farmacologia
Ratos
Sobrevivência de Tecidos/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Insect Proteins); 0 (Organ Preservation Solutions); EC 3.4.22.- (Calpain); EC 3.4.22.- (Caspase 3); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE


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[PMID]:28421488
[Au] Autor:Kim SK; Youm HW; Lee JR; Suh CS
[Ad] Endereço:Department of Obstetrics and Gynecology, Seoul National University Bundang Hospital, 82 Gumi-ro 173 Beon-gil Bundang-gu, Seongnam, 463-707, South Korea.
[Ti] Título:Chapter 4 Role of Antioxidants and Antifreeze Proteins in Cryopreservation/Vitrification.
[So] Source:Methods Mol Biol;1568:45-63, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In recent years, supplementation of antioxidants and antifreeze proteins during cryopreservation/vitrification has significantly improved the survival and function of oocytes and ovarian tissues (OT) in animal models. In this chapter, the experimental protocols for the use of antioxidants and antifreeze proteins in cryopreservation/vitrification are described.
[Mh] Termos MeSH primário: Proteínas Anticongelantes
Antioxidantes
Criopreservação/métodos
Crioprotetores
Oócitos
Ovário
Vitrificação
[Mh] Termos MeSH secundário: Animais
Proteínas Anticongelantes/farmacologia
Antioxidantes/farmacologia
Catalase/metabolismo
Diferenciação Celular
Criopreservação/instrumentação
Crioprotetores/farmacologia
Feminino
Preservação da Fertilidade
Fertilização In Vitro
Camundongos
Oócitos/citologia
Oócitos/efeitos dos fármacos
Oócitos/metabolismo
Ovário/citologia
Ovário/efeitos dos fármacos
Ovário/metabolismo
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Antioxidants); 0 (Cryoprotective Agents); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6828-2_4


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[PMID]:28134801
[Au] Autor:Kim HJ; Lee JH; Hur YB; Lee CW; Park SH; Koo BW
[Ad] Endereço:Department of Chemistry, Pukyong National University, Busan 48513, Korea. kimhj@pknu.ac.kr.
[Ti] Título:Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant.
[So] Source:Mar Drugs;15(2), 2017 Jan 27.
[Is] ISSN:1660-3397
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Antifreeze proteins (AFPs) are biological antifreezes with unique properties, including thermal hysteresis(TH),ice recrystallization inhibition(IRI),and interaction with membranes and/or membrane proteins. These properties have been utilized in the preservation of biological samples at low temperatures. Here, we review the structure and function of marine-derived AFPs, including moderately active fish AFPs and hyperactive polar AFPs. We also survey previous and current reports of cryopreservation using AFPs. Cryopreserved biological samples are relatively diverse ranging from diatoms and reproductive cells to embryos and organs. Cryopreserved biological samples mainly originate from mammals. Most cryopreservation trials using marine-derived AFPs have demonstrated that addition of AFPs can improve post-thaw viability regardless of freezing method (slow-freezing or vitrification), storage temperature, and types of biological sample type.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/metabolismo
Organismos Aquáticos/metabolismo
Crioprotetores/metabolismo
[Mh] Termos MeSH secundário: Animais
Criopreservação/métodos
Cristalização/métodos
Congelamento
Gelo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Cryoprotective Agents); 0 (Ice)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170616
[Lr] Data última revisão:
170616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170131
[St] Status:MEDLINE


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[PMID]:27936601
[Au] Autor:Stubbs C; Lipecki J; Gibson MI
[Ad] Endereço:Department of Chemistry and ‡Warwick Medical School, University of Warwick , Coventry, CV4 7AL, United Kingdom.
[Ti] Título:Regioregular Alternating Polyampholytes Have Enhanced Biomimetic Ice Recrystallization Activity Compared to Random Copolymers and the Role of Side Chain versus Main Chain Hydrophobicity.
[So] Source:Biomacromolecules;18(1):295-302, 2017 Jan 09.
[Is] ISSN:1526-4602
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Antifreeze proteins from polar fish species are potent ice recrystallization inhibitors (IRIs) effectively stopping all ice growth. Additives that have IRI activity have been shown to enhance cellular cryopreservation with potential to improve the distribution of donor cells and tissue. Polyampholytes, polymers with both anionic and cationic side chains, are a rapidly emerging class of polymer cryoprotectants, but their mode of action and the structural features essential for activity are not clear. Here regioregular polyampholytes are synthesized from maleic anhydride copolymers to enable stoichiometric installation of the charged groups, ensuring regioregularity, which is not possible using conventional random copolymerization. A modular synthetic strategy is employed to enable the backbone and side chain hydrophobicity to be varied, with side chain hydrophobicity found to have a profound effect on the IRI activity. The activity of the regioregular polymers was found to be superior to those derived from a standard random copolymerization with statistical incorporation of monomers, demonstrating that sequence composition is crucial to the activity of IRI active polyampholytes.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/química
Crioprotetores/química
Gelo
Anidridos Maleicos/química
Polímeros/química
[Mh] Termos MeSH secundário: Biomimética
Cristalização
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Cryoprotective Agents); 0 (Ice); 0 (Maleic Anhydrides); 0 (Polymers)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biomac.6b01691


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[PMID]:27860412
[Au] Autor:Mangiagalli M; Bar-Dolev M; Tedesco P; Natalello A; Kaleda A; Brocca S; de Pascale D; Pucciarelli S; Miceli C; Bravslavsky I; Lotti M
[Ad] Endereço:Department of Biotechnology and Biosciences, State University of Milano-Bicocca, Italy.
[Ti] Título:Cryo-protective effect of an ice-binding protein derived from Antarctic bacteria.
[So] Source:FEBS J;284(1):163-177, 2017 Jan.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cold environments are populated by organisms able to contravene deleterious effects of low temperature by diverse adaptive strategies, including the production of ice binding proteins (IBPs) that inhibit the growth of ice crystals inside and outside cells. We describe the properties of such a protein (EfcIBP) identified in the metagenome of an Antarctic biological consortium composed of the ciliate Euplotes focardii and psychrophilic non-cultured bacteria. Recombinant EfcIBP can resist freezing without any conformational damage and is moderately heat stable, with a midpoint temperature of 66.4 °C. Tested for its effects on ice, EfcIBP shows an unusual combination of properties not reported in other bacterial IBPs. First, it is one of the best-performing IBPs described to date in the inhibition of ice recrystallization, with effective concentrations in the nanomolar range. Moreover, EfcIBP has thermal hysteresis activity (0.53 °C at 50 µm) and it can stop a crystal from growing when held at a constant temperature within the thermal hysteresis gap. EfcIBP protects purified proteins and bacterial cells from freezing damage when exposed to challenging temperatures. EfcIBP also possesses a potential N-terminal signal sequence for protein transport and a DUF3494 domain that is common to secreted IBPs. These features lead us to hypothesize that the protein is either anchored at the outer cell surface or concentrated around cells to provide survival advantage to the whole cell consortium.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/química
Bactérias/química
Euplotes/química
Gelo/análise
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Sequência de Aminoácidos
Regiões Antárticas
Proteínas Anticongelantes/genética
Proteínas Anticongelantes/metabolismo
Organismos Aquáticos
Bactérias/genética
Bactérias/metabolismo
Sítios de Ligação
Clonagem Molecular
Temperatura Baixa
Escherichia coli/genética
Escherichia coli/metabolismo
Euplotes/genética
Euplotes/metabolismo
Expressão Gênica
Cinética
Metagenoma
Modelos Moleculares
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Sinais Direcionadores de Proteínas
Estabilidade Proteica
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Ice); 0 (Protein Sorting Signals); 0 (Recombinant Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170622
[Lr] Data última revisão:
170622
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1111/febs.13965


  8 / 781 MEDLINE  
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[PMID]:27847317
[Au] Autor:Buch JL; Ramløv H
[Ad] Endereço:Department of Science and Environment, Roskilde University, Universitetsvej 1, 4000, Roskilde, Denmark. Electronic address: jloerup@gmail.com.
[Ti] Título:Detecting seasonal variation of antifreeze protein distribution in Rhagium mordax using immunofluorescence and high resolution microscopy.
[So] Source:Cryobiology;74:132-140, 2017 Feb.
[Is] ISSN:1090-2392
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Larvae of the blackspotted pliers support beetle, Rhagium mordax, were collected monthly, for the duration of 2012 and fixed. The larvae were embedded in paraffin wax and sectioned. Using fluorophore-coupled antibodies specific to the R. mordax antifreeze protein, RmAFP1, sections were visualised with UV reflected light microscopy. An automated software analysis method was developed in order to discard autofluorescence, and quantify fluorescence from bound antibodies. The results show that R. mordax cuticle and gut exhibit a higher degree of fluorophore-bound fluorescence during summer, than in the cold months. It is hypothesised that R. mordax stores RmAFP1 in, or near, the fat body during times when freeze avoidance is not needed.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/metabolismo
Coleópteros/metabolismo
Larva/metabolismo
[Mh] Termos MeSH secundário: Animais
Imunofluorescência
Congelamento
Microscopia
Estações do Ano
Coloração e Rotulagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifreeze Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161117
[St] Status:MEDLINE


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[PMID]:27739374
[Au] Autor:Cheung RCF; Ng TB; Wong JH
[Ad] Endereço:School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Hong Kong, China.
[Ti] Título:Antifreeze Proteins from Diverse Organisms and their Applications: An Overview.
[So] Source:Curr Protein Pept Sci;18(3):262-283, 2017.
[Is] ISSN:1875-5550
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Antifreeze proteins are ice-binding or ice-structuring proteins that prevent water from freezing by adsorbing to the ice surface and stopping the growth of minute ice crystals to large crystals in a non-colligative manner. The antifreeze proteins are found in species like fish, arthropods, plants, algae, fungi, yeasts and bacteria. The diversity, distribution and classification of antifreeze proteins were highlighted in this review. Antifreeze proteins help the organisms adapt to and survive in subzero temperature environments. The distribution of antifreeze proteins in different species appears to be the outcome of a combination of independent evolutionary events, probably the convergent evolution or horizontal gene transfer. Benefits can be derived from the frost resistance of these organisms. Their potential applications have been recognized in food processing, cryopreservation, cryosurgery, fishery and agricultural industries and anti-icing materials development. This review includes information on the current understanding of antifreeze proteins. A discussion on interactions and mechanisms involving ice recognition and adsorption was also included.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/química
Proteínas Anticongelantes/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Criopreservação/métodos
Evolução Molecular
Proteínas de Peixes/química
Proteínas de Peixes/metabolismo
Aditivos Alimentares/química
Manipulação de Alimentos
Proteínas Fúngicas/química
Proteínas Fúngicas/metabolismo
Proteínas de Insetos/química
Proteínas de Insetos/metabolismo
Marinomonas/química
Proteínas de Plantas/química
Proteínas de Plantas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Bacterial Proteins); 0 (Fish Proteins); 0 (Food Additives); 0 (Fungal Proteins); 0 (Insect Proteins); 0 (Plant Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161015
[St] Status:MEDLINE
[do] DOI:10.2174/1389203717666161013095027


  10 / 781 MEDLINE  
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[PMID]:27737617
[Au] Autor:Kim EJ; Lee JH; Lee SG; Han SJ
[Ad] Endereço:a Division of Life Sciences , Korea Polar Research Institute, Korea Institute of Ocean Science and Technology , Incheon , South Korea.
[Ti] Título:Improving thermal hysteresis activity of antifreeze protein from recombinant Pichia pastoris by removal of N-glycosylation.
[So] Source:Prep Biochem Biotechnol;47(3):299-304, 2017 Mar 16.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To survive in a subzero environment, polar organisms produce ice-binding proteins (IBPs). These IBPs prevent the formation of large intracellular ice crystals, which may be fatal to the organism. Recently, a recombinant FfIBP (an IBP from Flavobacterium frigoris PS1) was cloned and produced in Pichia pastoris using fed-batch fermentation with methanol feeding. In this study, we demonstrate that FfIBP produced by P. pastoris has a glycosylation site, which diminishes the thermal hysteresis activity of FfIBP. The FfIBP expressed by P. pastoris exhibited a doublet on SDS-PAGE. The results of a glycosidase reaction suggested that FfIBP possesses complex N-linked oligosaccharides. These results indicate that the residues of the glycosylated site could disturb the binding of FfIBP to ice molecules. The findings of this study could be utilized to produce highly active antifreeze proteins on a large scale.
[Mh] Termos MeSH primário: Proteínas Anticongelantes/genética
Proteínas Anticongelantes/metabolismo
Flavobacterium/genética
Gelo/análise
Pichia/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Anticongelantes/química
Clonagem Molecular
Fermentação
Flavobacterium/química
Flavobacterium/metabolismo
Glicosilação
Modelos Moleculares
Pichia/química
Pichia/metabolismo
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifreeze Proteins); 0 (Ice); 0 (Recombinant Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170324
[Lr] Data última revisão:
170324
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161015
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2016.1244682



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde