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  1 / 6811 MEDLINE  
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[PMID]:29288668
[Au] Autor:Groves MR; Schroer CFE; Middleton AJ; Lunev S; Danda N; Ali AM; Marrink SJ; Williams C
[Ad] Endereço:Department of Drug Design, Groningen Research Institute of Pharmacy, University of Groningen, 9713AV, The Netherlands.
[Ti] Título:Structural insights into K48-linked ubiquitin chain formation by the Pex4p-Pex22p complex.
[So] Source:Biochem Biophys Res Commun;496(2):562-567, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pex4p is a peroxisomal E2 involved in ubiquitinating the conserved cysteine residue of the cycling receptor protein Pex5p. Previously, we demonstrated that Pex4p from the yeast Saccharomyces cerevisiae binds directly to the peroxisomal membrane protein Pex22p and that this interaction is vital for receptor ubiquitination. In addition, Pex22p binding allows Pex4p to specifically produce lysine 48 linked ubiquitin chains in vitro through an unknown mechanism. This activity is likely to play a role in targeting peroxisomal proteins for proteasomal degradation. Here we present the crystal structures of Pex4p alone and in complex with Pex22p from the yeast Hansenula polymorpha. Comparison of the two structures demonstrates significant differences to the active site of Pex4p upon Pex22p binding while molecular dynamics simulations suggest that Pex22p binding facilitates active site remodelling of Pex4p through an allosteric mechanism. Taken together, our data provide insights into how Pex22p binding allows Pex4p to build K48-linked Ub chains.
[Mh] Termos MeSH primário: Proteínas Fúngicas/metabolismo
Peroxinas/metabolismo
Pichia/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Proteínas Fúngicas/química
Modelos Moleculares
Peroxinas/química
Pichia/química
Ligação Proteica
Conformação Proteica
Ubiquitinação
Ubiquitinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Peroxins); 0 (Ubiquitins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE


  2 / 6811 MEDLINE  
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[PMID]:29339156
[Au] Autor:Zhang M; Wu W; Chen Z
[Ad] Endereço:Beijing Advanced Innovation Center for Food Nutrition and Human Health, State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
[Ti] Título:Structure and function of cytoplasmic serine hydroxymethyltransferase from Pichia pastoris.
[So] Source:Biochem Biophys Res Commun;496(2):753-757, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serine hydroxymethyltransferase (SHMT) catalyzes the interconversion of serine and glycine, which is crucial for one carbon metabolism. Here, we report the first crystal structure of cytoplasmic SHMT from Pichia pastoris (pcSHMT) diffracted to 2.5 Šresolution in space group C222 . PcSHMT was a contaminant with our target protein expressed in Pichia pastoris and confirmed by mass spectrometry. The overall structure of pcSHMT is similar to Human mitochondrial SHMT and different to E. coli SHMT. Interestingly, the oligomerization of pcSHMT expressed in eukaryotic or prokaryotic system differs significantly and is regulated by pyridoxal-5'-phosphate. Our results revealed a close evolutionary relationship between Pichia pastoris and Human mitochondria.
[Mh] Termos MeSH primário: Glicina Hidroximetiltransferase/metabolismo
Pichia/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalografia por Raios X
Glicina Hidroximetiltransferase/química
Seres Humanos
Modelos Moleculares
Pichia/química
Pichia/citologia
Pichia/metabolismo
Conformação Proteica
Multimerização Proteica
Fosfato de Piridoxal/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
5V5IOJ8338 (Pyridoxal Phosphate); EC 2.1.2.1 (Glycine Hydroxymethyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  3 / 6811 MEDLINE  
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[PMID]:28745425
[Au] Autor:Filipov Y; Domanskyi S; Wood ML; Gamella M; Privman V; Katz E
[Ad] Endereço:Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, 13699, USA.
[Ti] Título:Experimental Realization of a High-Quality Biochemical XOR Gate.
[So] Source:Chemphyschem;18(20):2908-2915, 2017 Oct 19.
[Is] ISSN:1439-7641
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We report an experimental realization of a biochemical XOR gate function that avoids many of the pitfalls of earlier realizations based on biocatalytic cascades. Inputs-represented by pairs of chemicals-cross-react to largely cancel out when both are nearly equal. The cross-reaction can be designed to also optimize gate functioning for noise handling. When not equal, the residual inputs are further processed to result in the output of the XOR type, by biocatalytic steps that allow for further gate-function optimization. The quality of the realized XOR gate is theoretically analyzed.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Oxirredutases do Álcool/metabolismo
Biocatálise
Glucose Oxidase/metabolismo
Hexoquinase/metabolismo
NAD/metabolismo
Peroxidase/metabolismo
[Mh] Termos MeSH secundário: Armoracia/enzimologia
Aspergillus niger/enzimologia
Modelos Moleculares
Pichia/enzimologia
Saccharomyces cerevisiae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0U46U6E8UK (NAD); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.1.3.13 (alcohol oxidase); EC 1.1.3.4 (Glucose Oxidase); EC 1.11.1.7 (Peroxidase); EC 2.7.1.1 (Hexokinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1002/cphc.201700705


  4 / 6811 MEDLINE  
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[PMID]:29337064
[Au] Autor:Knollenberg BJ; Liu J; Yu S; Lin H; Tian L
[Ad] Endereço:Department of Plant Sciences, University of California, Davis, CA, 95616, USA; The Huck Institutes of the Life Sciences, Pennsylvania State University, State College, PA, 16801, USA.
[Ti] Título:Cloning and functional characterization of a p-coumaroyl quinate/shikimate 3'-hydroxylase from potato (Solanum tuberosum).
[So] Source:Biochem Biophys Res Commun;496(2):462-467, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chlorogenic acid (CGA) plays an important role in protecting plants against pathogens and promoting human health. Although CGA accumulates to high levels in potato tubers, the key enzyme p-coumaroyl quinate/shikimate 3'-hydroxylase (C3'H) for CGA biosynthesis has not been isolated and functionally characterized in potato. In this work, we cloned StC3'H from potato and showed that it catalyzed the formation of caffeoylshikimate and CGA (caffeoylquinate) from p-coumaroyl shikimate and p-coumaroyl quinate, respectively, but was inactive towards p-coumaric acid in in vitro enzyme assays. When the expression of StC3'H proteins was blocked through antisense (AS) inhibition under the control of a tuber-specific patatin promoter, moderate changes in tuber yield as well as phenolic metabolites in the core tuber tissue were observed for several AS lines. On the other hand, the AS and control potato lines exhibited similar responses to a bacterial pathogen Pectobacterium carotovorum. These results suggest that StC3'H is implicated in phenolic metabolism in potato. They also suggest that CGA accumulation in the core tissue of potato tubers is an intricately controlled process and that additional C3'H activity may also be involved in CGA biosynthesis in potato.
[Mh] Termos MeSH primário: Ácido Clorogênico/metabolismo
Oxigenases de Função Mista/genética
Proteínas de Plantas/genética
Tubérculos/enzimologia
Solanum tuberosum/enzimologia
[Mh] Termos MeSH secundário: Hidrolases de Éster Carboxílico/genética
Hidrolases de Éster Carboxílico/metabolismo
Ácido Clorogênico/análogos & derivados
Clonagem Molecular
Expressão Gênica
Oxigenases de Função Mista/antagonistas & inibidores
Oxigenases de Função Mista/metabolismo
Oligonucleotídeos Antissenso/genética
Oligonucleotídeos Antissenso/metabolismo
Pectobacterium carotovorum/patogenicidade
Pectobacterium carotovorum/fisiologia
Pichia/genética
Pichia/metabolismo
Proteínas de Plantas/metabolismo
Tubérculos/genética
Tubérculos/microbiologia
Plantas Geneticamente Modificadas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ácido Chiquímico/análogos & derivados
Ácido Chiquímico/metabolismo
Solanum tuberosum/genética
Solanum tuberosum/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (4-coumaroylshikimic acid); 0 (Oligonucleotides, Antisense); 0 (Plant Proteins); 0 (Recombinant Proteins); 0 (patatin protein, Solanum tuberosum); 29MS2WI2NU (Shikimic Acid); 318ADP12RI (Chlorogenic Acid); 73263-62-4 (5-O-caffeoylshikimic acid); E57A0DKE0B (3,4-di-O-caffeoylquinic acid); EC 1.- (Mixed Function Oxygenases); EC 1.14.13.- (5-O-(4-coumaroyl)shikimate 3'-hydroxylase); EC 3.1.1.- (Carboxylic Ester Hydrolases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE


  5 / 6811 MEDLINE  
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[PMID]:29305978
[Au] Autor:Lin J; Xia X; Yu XQ; Shen J; Li Y; Lin H; Tang S; Vasseur L; You M
[Ad] Endereço:State Key Laboratory of Ecological Pest Control for Fujian/Taiwan Crops and College of Life Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China; Institute of Applied Ecology, Fujian Agriculture and Forestry University, Fuzhou 350002, China; Fujian Vocational College of Bioengin
[Ti] Título:Gene expression profiling provides insights into the immune mechanism of Plutella xylostella midgut to microbial infection.
[So] Source:Gene;647:21-30, 2018 Mar 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Insect gut immunity plays a key role in defense against microorganism infection. The knowledge of insect gut immunity has been obtained mostly from Drosophila melanogaster. Little is known about gut immunity in the diamondback moth, Plutella xylostella (L.), a pest destroying cruciferous crops worldwide. In this study, expressions of the immune-related genes in the midgut of P. xylostella orally infected with Staphylococcus aureus, Escherichia coli and Pichia pastoris were profiled by RNA-seq and qRT-PCR approaches. The results revealed that the Toll, IMD, JNK and JAK-STAT pathways and possibly the prophenoloxidase activation system in P. xylostella could be activated by oral infections, and moricins, gloverins and lysozyme2 might act as important effectors against microorganisms. Subsequent knock-down of IMD showed that this gene was involved in regulating the expression of down-stream genes in the IMD pathway. Our work indicates that the Toll, IMD, JNK and JAK-STAT pathways may synergistically modulate immune responses in the P. xylostella midgut, implying a complex and diverse immune system in the midgut of insects.
[Mh] Termos MeSH primário: Sistema Digestório/microbiologia
Infecções por Escherichia coli/genética
Lepidópteros/genética
Lepidópteros/imunologia
Micoses/genética
Infecções Estafilocócicas/genética
Transcriptoma/genética
[Mh] Termos MeSH secundário: Animais
Escherichia coli/imunologia
Infecções por Escherichia coli/imunologia
Perfilação da Expressão Gênica/métodos
Proteínas de Insetos/genética
Lepidópteros/microbiologia
Mariposas/genética
Mariposas/imunologia
Mariposas/microbiologia
Micoses/imunologia
Pichia/imunologia
Transdução de Sinais/genética
Transdução de Sinais/imunologia
Infecções Estafilocócicas/imunologia
Staphylococcus aureus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180107
[St] Status:MEDLINE


  6 / 6811 MEDLINE  
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[PMID]:28470625
[Au] Autor:Martínez-Hernández SL; Cervantes-García D; Muñoz-Ortega M; Aldaba-Muruato LR; Loera-Muro VM; Ascacio-Martínez JA; de Jesús Loera-Arias M; de Oca-Luna RM; Ventura-Juárez J
[Ad] Endereço:Departamento de Morfología, Centro de Ciencias Básicas, Universidad Autónoma de Aguascalientes, Av. Universidad # 940, Ciudad Universitaria, C. P. 20131, Aguascalientes, AGS, Mexico.
[Ti] Título:An anti-amoebic vaccine: generation of the recombinant antigen LC3 from Entamoeba histolytica linked to mutated exotoxin A (PEΔIII) via the Pichia pastoris system.
[So] Source:Biotechnol Lett;39(8):1149-1157, 2017 Aug.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To generate an immunogenic chimeric protein containing the Entamoeba histolytica LC3 fragment fused to the retrograde delivery domains of exotoxin A of Pseudomonas aeruginosa and KDEL3 for use as an effective vaccine. RESULTS: A codon-optimized synthetic gene encoding the PEΔIII-LC3-KDEL3 fusion construct was designed for expression in Pichia pastoris. This transgene was subcloned into the plasmid pPIC9 for methanol-inducible expression. After transformation and selection of positive-transformed clones by PCR, the expression of the recombinant protein PEΔIII-LC3-KDEL3 was elicited. SDS-PAGE, protein glycosylation staining and western blot assays demonstrated a 67 kDa protein in the medium culture supernatant. The recombinant protein was detected with a polyclonal anti-6X His tag antibody and a polyclonal E. histolytica-specific antibody. A specific antibody response was induced in hamsters after immunization with this protein. CONCLUSIONS: We report for the first time the design and expression of the recombinant E. histolytica LC3 protein fused to PEΔIII and KDEL3, with potential application as an immunogen.
[Mh] Termos MeSH primário: ADP Ribose Transferases/genética
Toxinas Bacterianas/genética
Entamoeba histolytica/genética
Exotoxinas/genética
Proteínas Recombinantes de Fusão/genética
Vacinas
Fatores de Virulência/genética
[Mh] Termos MeSH secundário: ADP Ribose Transferases/imunologia
Animais
Toxinas Bacterianas/imunologia
Entamoeba histolytica/imunologia
Exotoxinas/imunologia
Pichia/genética
Proteínas Recombinantes de Fusão/imunologia
Fatores de Virulência/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Exotoxins); 0 (Recombinant Fusion Proteins); 0 (Vaccines); 0 (Virulence Factors); EC 2.4.2.- (ADP Ribose Transferases); EC 2.4.2.31 (toxA protein, Pseudomonas aeruginosa)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-017-2341-2


  7 / 6811 MEDLINE  
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[PMID]:29253895
[Au] Autor:Wang X; Zheng F; Wang Y; Tu T; Ma R; Su X; You S; Yao B; Xie X; Luo H
[Ad] Endereço:College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, People's Republic of China.
[Ti] Título:Improvement of the catalytic efficiency of a hyperthermophilic xylanase from Bispora sp. MEY-1.
[So] Source:PLoS One;12(12):e0189806, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extremophilic xylanases have attracted great scientific and industrial interest. In this study, a GH10 xylanase-encoding gene, Xyl10E, was cloned from Bispora sp. MEY-1 and expressed in Pichia pastoris GS115. Deduced Xyl10E shares the highest identities of 62% and 57% with characterized family GH10 xylanases from Talaromyces leycettanus and Penicillium canescens (structure 4F8X), respectively. Xyl10E was most active at 93 to 95°C and pH 4.0, retained more than 75% or 48% of the initial activity when heated at 80°C or 90°C for 30 min, respectively, and hardly lost activity at pH 1.0 to 7.0, but was completely inhibited by SDS. Two residues, A160 and A161, located on loop 4, were identified to play roles in catalysis. Mutants A160D/E demonstrated higher affinity to substrate with lower Km values, while mutants A161D/E mainly displayed elevated Vmax values. All of these mutants had significantly improved catalytic efficiency. According to the molecular dynamics simulation, the mutation of A160E was able to affect the important substrate binding site Y204 and then improve the substrate affinity, and the mutation of A161D was capable of forming a hydrogen bond with the substrate to promote the substrate binding or accelerate the product release. This study introduces a highly thermophilic fungal xylanase and reveals the importance of loop 4 for catalytic efficiency.
[Mh] Termos MeSH primário: Ascomicetos/enzimologia
Endo-1,4-beta-Xilanases/metabolismo
[Mh] Termos MeSH secundário: Ascomicetos/genética
Catálise
Domínio Catalítico
Clonagem Molecular
Estabilidade Enzimática
Proteínas Fúngicas/metabolismo
Ligações de Hidrogênio
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Simulação de Dinâmica Molecular
Mutagênese
Mutagênese Sítio-Dirigida
Mutação
Pichia/genética
Pichia/metabolismo
Proteínas Recombinantes/metabolismo
Talaromyces/metabolismo
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Recombinant Proteins); 0 (Xylans); EC 3.2.1.8 (Endo-1,4-beta Xylanases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189806


  8 / 6811 MEDLINE  
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[PMID]:29228039
[Au] Autor:Liu B; Olson Å; Wu M; Broberg A; Sandgren M
[Ad] Endereço:Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala, Sweden.
[Ti] Título:Biochemical studies of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare and their roles in lignocellulose degradation.
[So] Source:PLoS One;12(12):e0189479, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lytic polysaccharide monooxygenases (LPMO) are important redox enzymes produced by microorganisms for the degradation of recalcitrant natural polysaccharides. Heterobasidion irregulare is a white-rot phytopathogenic fungus that causes wood decay in conifers. The genome of this fungus encodes 10 putative Auxiliary Activity family 9 (AA9) LPMOs. We describe the first biochemical characterization of H. irregulare LPMOs through heterologous expression of two CBM-containing LPMOs from this fungus (HiLPMO9H, HiLPMO9I) in Pichia pastoris. The oxidization preferences and substrate specificities of these two enzymes were determined. The two LPMOs were shown to cleave different carbohydrate components of plant cell walls. HiLPMO9H was active on cellulose and oxidized the substrate at the C1 carbon of the pyranose ring at ß-1,4-glycosidic linkages, whereas HiLPMO9I cleaved cellulose with strict oxidization at the C4 carbon of glucose unit at internal bonds, and also showed activity against glucomannan. We propose that the two LPMOs play different roles in the plant-cell-wall degrading system of H. irregulare for degradation of softwood and that the lignocellulose degradation mediated by this white-rot fungus may require collective efforts from multi-types of LPMOs.
[Mh] Termos MeSH primário: Basidiomycota/enzimologia
Lignina/metabolismo
Oxigenases de Função Mista/metabolismo
Polissacarídeos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cromatografia Líquida de Alta Pressão
Cromatografia por Troca Iônica
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Oxigenases de Função Mista/química
Pichia/genética
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polysaccharides); 11132-73-3 (lignocellulose); 9005-53-2 (Lignin); EC 1.- (Mixed Function Oxygenases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189479


  9 / 6811 MEDLINE  
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[PMID]:28543537
[Au] Autor:Durante M; Tufariello M; Tommasi L; Lenucci MS; Bleve G; Mita G
[Ad] Endereço:Istituto di Scienze delle Produzioni Alimentari (ISPA)-CNR, Lecce, Italy.
[Ti] Título:Evaluation of bioactive compounds in black table olives fermented with selected microbial starters.
[So] Source:J Sci Food Agric;98(1):96-103, 2018 Jan.
[Is] ISSN:1097-0010
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Table olives have been a component of the Mediterranean diet for centuries, with the trend for their consumption currently increasing worldwide. They are rich in bioactive molecules with nutritional, antioxidant, anti-inflammatory or hormone-like properties. In the present study, the concentrations of phenolics, triterpenic acids, carotenoids and vitamins, as well as fatty acid profiles and antioxidant activity, were analyzed in the edible portion of black table olives (Olea europea L.) from Italian (Cellina di Nardò and Leccino) and Greek (Kalamàta and Conservolea) cultivars fermented with selected autochthonous starters and in the corresponding monovarietal olive oils. RESULTS: On a fresh weight basis, Cellina di Nardò and Leccino table olives showed the highest total phenolic content. No significant differences were found with respect to the levels of total triterpenic (maslinic and oleanolic) acids and vitamin E among cultivars. All table olives were characterized by high amounts of oleic, linoleic and palmitic acids. Oils were richer in lipophilic antioxidants (carotenoids and tocochromanols) than table olives, which, instead, showed a higher content of polyphenols and triterpenic acids than oils. CONCLUSION: The present study demonstrates that fermented table olives are an excellent natural source of unsaturated fatty acids, as well as being nutritionally important health-promoting bioactive compounds. © 2017 Society of Chemical Industry.
[Mh] Termos MeSH primário: Frutas/química
Lactobacillus plantarum/metabolismo
Olea/microbiologia
Pichia/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Antioxidantes/análise
Antioxidantes/metabolismo
Ácidos Graxos Insaturados/análise
Ácidos Graxos Insaturados/metabolismo
Fermentação
Frutas/metabolismo
Frutas/microbiologia
Grécia
Itália
Olea/química
Olea/metabolismo
Polifenóis/análise
Polifenóis/metabolismo
Vitamina E/análise
Vitamina E/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Fatty Acids, Unsaturated); 0 (Polyphenols); 1406-18-4 (Vitamin E)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1002/jsfa.8443


  10 / 6811 MEDLINE  
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[PMID]:29185908
[Au] Autor:Prabhu AA; Venkata Dasu V
[Ad] Endereço:a Department of Biosciences and Bioengineering , Biochemical Engineering Laboratory, Indian Institute of Technology Guwahati , Guwahati , Assam , India.
[Ti] Título:Dual-substrate inhibition kinetic studies for recombinant human interferon gamma producing Pichia pastoris.
[So] Source:Prep Biochem Biotechnol;47(10):953-962, 2017 Nov 26.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pichia pastoris is considered as one of the prominent host extensively used as a platform for heterologous protein production. In the present study, the growth inhibition kinetics of recombinant P. pastoris expressing human interferon gamma was studied under different initial substrate concentrations of gluconate (10-100 g L ) and methanol (2-50 g L ) in modified FM22 medium. The highest specific growth rate of 0.0206 and 0.019 hr was observed at 60 g L of gluconate and 10 g L of methanol, respectively. Various three- and four-parametric Monod-variant models were chosen to analyze the inhibition kinetics. The model parameters as well as goodness of fit were estimated using nonlinear regression analysis. The three-parameter Haldane model was found to be best fit for both gluconate (R = 0.95) and methanol substrate (R = 0.96). The parameter sensitivity analysis revealed that µ , K , and K are the most sensitive parameters for both methanol and gluconate. Different substrate inhibition models were fitted to the growth kinetic data and the additive form of double Webb model was found to be the best to explain the growth kinetics of recombinant P. pastoris.
[Mh] Termos MeSH primário: Gluconatos/metabolismo
Microbiologia Industrial/métodos
Interferon gama/metabolismo
Metanol/metabolismo
Pichia/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Meios de Cultura/metabolismo
Seres Humanos
Cinética
Pichia/metabolismo
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (Gluconates); 0 (IFNG protein, human); 0 (Recombinant Proteins); 82115-62-6 (Interferon-gamma); R4R8J0Q44B (gluconic acid); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1350977



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