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[PMID]:27998268
[Au] Autor:Seppälä S; Solomon KV; Gilmore SP; Henske JK; O'Malley MA
[Ad] Endereço:Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kemitorvet Bygning 220, 2800, Kgs. Lyngby, Denmark.
[Ti] Título:Mapping the membrane proteome of anaerobic gut fungi identifies a wealth of carbohydrate binding proteins and transporters.
[So] Source:Microb Cell Fact;15(1):212, 2016 Dec 20.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Engineered cell factories that convert biomass into value-added compounds are emerging as a timely alternative to petroleum-based industries. Although often overlooked, integral membrane proteins such as solute transporters are pivotal for engineering efficient microbial chassis. Anaerobic gut fungi, adapted to degrade raw plant biomass in the intestines of herbivores, are a potential source of valuable transporters for biotechnology, yet very little is known about the membrane constituents of these non-conventional organisms. Here, we mined the transcriptome of three recently isolated strains of anaerobic fungi to identify membrane proteins responsible for sensing and transporting biomass hydrolysates within a competitive and rather extreme environment. RESULTS: Using sequence analyses and homology, we identified membrane protein-coding sequences from assembled transcriptomes from three strains of anaerobic gut fungi: Neocallimastix californiae, Anaeromyces robustus, and Piromyces finnis. We identified nearly 2000 transporter components: about half of these are involved in the general secretory pathway and intracellular sorting of proteins; the rest are predicted to be small-solute transporters. Unexpectedly, we found a number of putative sugar binding proteins that are associated with prokaryotic uptake systems; and approximately 100 class C G-protein coupled receptors (GPCRs) with non-canonical putative sugar binding domains. CONCLUSIONS: We report the first comprehensive characterization of the membrane protein machinery of biotechnologically relevant anaerobic gut fungi. Apart from identifying conserved machinery for protein sorting and secretion, we identify a large number of putative solute transporters that are of interest for biotechnological applications. Notably, our data suggests that the fungi display a plethora of carbohydrate binding domains at their surface, perhaps as a means to sense and sequester some of the sugars that their biomass degrading, extracellular enzymes produce.
[Mh] Termos MeSH primário: Carboidratos
Proteínas Fúngicas/metabolismo
Fungos/metabolismo
Intestinos/microbiologia
Proteínas de Membrana/metabolismo
Proteoma/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Animais
Fezes/microbiologia
Proteínas Fúngicas/genética
Fungos/classificação
Fungos/genética
Perfilação da Expressão Gênica/métodos
Cabras
Cavalos
Lignina/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Neocallimastigales/genética
Neocallimastigales/metabolismo
Piromyces/genética
Piromyces/metabolismo
Ligação Proteica
Proteoma/genética
Ovinos
Especificidade da Espécie
Transcriptoma/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbohydrates); 0 (Fungal Proteins); 0 (Membrane Proteins); 0 (Membrane Transport Proteins); 0 (Proteome); 11132-73-3 (lignocellulose); 9005-53-2 (Lignin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170410
[Lr] Data última revisão:
170410
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161222
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-016-0611-7


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[PMID]:27287262
[Au] Autor:Li Y; Jin W; Cheng Y; Zhu W
[Ad] Endereço:Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, Laboratory of Gastrointestinal Microbiology, Nanjing Agricultural University, Nanjing, 210095, China.
[Ti] Título:Effect of the Associated Methanogen Methanobrevibacter thaueri on the Dynamic Profile of End and Intermediate Metabolites of Anaerobic Fungus Piromyces sp. F1.
[So] Source:Curr Microbiol;73(3):434-41, 2016 Sep.
[Is] ISSN:1432-0991
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although the scheme of metabolic pathways involved in the production of the major end products has been described, the dynamic profile of metabolites of anaerobic fungi co-cultured with methanogens is limited, especially for the intermediate metabolites. In the present study, the fermentation of the co-culture of Piromyces sp. F1 and Methanobrevibacter thaueri on glucose was investigated. The presence of methanogens shortened the growth lag time of anaerobic fungi and enhanced the total gas production. The occurrence of the maximum cell dry weight and the disappearance of most of the substrate were observed at 24 h for the co-culture and 48 h for the fungal mono-culture. In the co-culture, hydrogen was detected at a very low level during fermentation, and formate transitorily accumulated at 24 h and disappeared at 48 h, resulting in an increase of pH. Acetate was higher during the fermentation in the co-culture (P < 0.05), while lactate and ethanol were higher only in the initial stage of fermentation (P < 0.05). After 48 h, lactate in the mono-culture became much higher than that in the co-culture (P < 0.05), and ethanol tended to remain the same in both cultures. Moreover, malate tended to be exhausted in the co-culture, while it accumulated in the mono-culture. Citrate was also detected in both co-culture and mono-culture. Collectively, these results suggest that methanogen enhanced the malate pathway and weakened the lactate pathway of anaerobic fungus.
[Mh] Termos MeSH primário: Metano/metabolismo
Methanobrevibacter/metabolismo
Piromyces/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Técnicas de Cocultura
Fermentação
Glucose/metabolismo
Hidrogênio/metabolismo
Ácido Láctico/metabolismo
Malatos/metabolismo
Methanobrevibacter/crescimento & desenvolvimento
Piromyces/química
Piromyces/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Malates); 33X04XA5AT (Lactic Acid); 7YNJ3PO35Z (Hydrogen); 817L1N4CKP (malic acid); IY9XDZ35W2 (Glucose); OP0UW79H66 (Methane)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160612
[St] Status:MEDLINE
[do] DOI:10.1007/s00284-016-1078-9


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[PMID]:26160406
[Au] Autor:Hou J; Shen Y; Jiao C; Ge R; Zhang X; Bao X
[Ad] Endereço:The State Key Laboratory of Microbial Technology, Shandong University, Jinan, China.
[Ti] Título:Characterization and evolution of xylose isomerase screened from the bovine rumen metagenome in Saccharomyces cerevisiae.
[So] Source:J Biosci Bioeng;121(2):160-5, 2016 Feb.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The conversion of abundant levels of xylose in lignocellulosic materials into viable products would generate economic benefits. The heterologous expression of the xylose isomerase (XI) gene is considered a direct and effective strategy for establishing the xylose metabolic pathway in Saccharomyces cerevisiae. However, only limited sources of xylA are functionally expressed in S. cerevisiae and are capable of driving effective xylose consumption. In this study, Ru-xylA (where Ru represents the rumen), which was screened from the contents of the bovine rumen metagenomic library, was functionally expressed in S. cerevisiae, and the enzyme activity was 1.31 U mg(-1) protein. This is a new source of XI that can exhibit high activity levels in S. cerevisiae. The activity of this enzyme is comparable to those of the Piromyces sp. XI. Then, the Ru-XI activity was further improved through mutagenesis and growth-based screening in a centromeric plasmid. A variant containing two mutations (K11T/D220V) that exhibited a 68% increase in enzyme activity was isolated. Our work identified a new xylose isomerase that can be functionally expressed in S. cerevisiae and results in a higher XI enzyme activity through mutagenesis.
[Mh] Termos MeSH primário: Aldose-Cetose Isomerases/genética
Aldose-Cetose Isomerases/metabolismo
Evolução Biológica
Metagenoma/genética
Rúmen/enzimologia
Rúmen/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Animais
Bovinos
Expressão Gênica
Mutagênese
Proteínas Mutantes/química
Proteínas Mutantes/genética
Proteínas Mutantes/metabolismo
Mutação/genética
Piromyces/enzimologia
Saccharomyces cerevisiae/genética
Xilose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mutant Proteins); A1TA934AKO (Xylose); EC 5.3.1.- (Aldose-Ketose Isomerases); EC 5.3.1.5 (xylose isomerase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:160110
[Lr] Data última revisão:
160110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150711
[St] Status:MEDLINE


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[PMID]:25755016
[Au] Autor:Nkemka VN; Gilroyed B; Yanke J; Gruninger R; Vedres D; McAllister T; Hao X
[Ad] Endereço:Agriculture and Agri-Food Canada, Lethbridge Research Centre, 5403 1st Ave S. Lethbridge, Alberta T1J 4B1, Canada.
[Ti] Título:Bioaugmentation with an anaerobic fungus in a two-stage process for biohydrogen and biogas production using corn silage and cattail.
[So] Source:Bioresour Technol;185:79-88, 2015 Jun.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bioaugmentation with an anaerobic fungus, Piromyces rhizinflata YM600, was evaluated in an anaerobic two-stage system digesting corn silage and cattail. Comparable methane yields of 328.8±16.8mLg(-1)VS and 295.4±14.5mLg(-1)VS and hydrogen yields of 59.4±4.1mLg(-1)VS and 55.6±6.7mLg(-1)VS were obtained for unaugmented and bioaugmented corn silage, respectively. Similar CH4 yields of 101.0±4.8mLg(-1)VS and 104±19.1mLg(-1)VS and a low H2 yield (<1mLg(-1)VS) were obtained for unaugmented and bioaugmented cattail, respectively. However, bioaugmentation resulted in an initial increase in CH4 and H2 production rates and also increased volatile fatty acid degradation rate for both substrates. Our study demonstrates the potential of bioaugmentation with anaerobic fungus for improving the digestibility of lignocellulose substrates for biogas and biohydrogen production.
[Mh] Termos MeSH primário: Hidrogênio/metabolismo
Metano/metabolismo
Piromyces/metabolismo
Silagem/microbiologia
Typhaceae/microbiologia
Zea mays/microbiologia
[Mh] Termos MeSH secundário: Reatores Biológicos/microbiologia
Hidrogênio/isolamento & purificação
Lignina/metabolismo
Metano/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
11132-73-3 (lignocellulose); 7YNJ3PO35Z (Hydrogen); 9005-53-2 (Lignin); OP0UW79H66 (Methane)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150422
[Lr] Data última revisão:
150422
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150311
[St] Status:MEDLINE


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[PMID]:25495284
[Au] Autor:Lee SM; Guan LL; Eun JS; Kim CH; Lee SJ; Kim ET; Lee SS
[Ad] Endereço:Division of Applied Life Sciences (BK21+), Institute of Agriculture & Life Sciences, Graduate School of Gyeongsang National University, Jinju, Korea.
[Ti] Título:The effect of anaerobic fungal inoculation on the fermentation characteristics of rice straw silages.
[So] Source:J Appl Microbiol;118(3):565-73, 2015 Mar.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: To identify whether the supplement of anaerobic fungi isolates with cellulolytic activities accelerates the silage fermentation. METHODS AND RESULTS: Three fungal isolates with the highest cellulolytic activities among 45 strains of anaerobic fungal stock in our laboratory were selected and used as silage inoculants. The rice straw (RS) was ensiled for 10, 30, 60, 90 and 120 days with four treatments of anaerobic fungi derived from the control (no fungus), Piromyces M014 (isolated from the rumen of the Korean native goat), Orpinomyces R001 (isolated from the duodenum of Korean native cattle) and Neocallimastix M010 (isolated from the guts of termites), respectively. The silages inoculated with pure strains of fungi showed a higher fungal population (P < 0.05) when compared to the control silage. In situ ruminal DM disappearance of RS silage (RSS) was improved with fungal treatment. SEM observation showed live fungal cells inoculated in RS could survive during the ensiling process. Overall, this study indicated that the inoculation of anaerobic fungi decreased the cell wall content of the RSS and increased in situ dry matter disappearance. CONCLUSIONS: The supplementation of anaerobic fungi isolates to RSS as a silage inoculant improves the RSS quality. SIGNIFICANCE AND IMPACT OF THE STUDY: This is the first study showing the potential application of supplement of anaerobic fungi isolated from the guts may be applied industrially as an alternate feed additive that improves the silage quality.
[Mh] Termos MeSH primário: Fermentação
Fungos/metabolismo
Oryza
Silagem
[Mh] Termos MeSH secundário: Anaerobiose
Animais
Bovinos
Neocallimastigales/isolamento & purificação
Neocallimastix/isolamento & purificação
Piromyces/isolamento & purificação
Rúmen/microbiologia
Silagem/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1510
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141216
[St] Status:MEDLINE
[do] DOI:10.1111/jam.12724


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[PMID]:24670042
[Au] Autor:Tseng CW; Yeh DJ; Chuang FT; Lee SC; Liu JR
[Ad] Endereço:a Institute of Biotechnology , National Taiwan University , Taipei , Taiwan.
[Ti] Título:Immobilization of Piromyces rhizinflata ß-glucanase on poly(dimethylsiloxane) and Si wafer and prediction of optimum reaction for enzyme activity.
[So] Source:Prep Biochem Biotechnol;45(1):42-55, 2015.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:EglA, a ß-1,4-glucanase isolated from the ruminal fungus Piromyces rhizinflata, shows promise in a wide range of industrial applications because of its broad substrate specificity. In this study, EglA was immobilized on different supporting materials including poly(dimethylsiloxane) (PDMS), Si wafer, textured Si wafer, and indium tin oxide-coated (ITO-coated) glass. The binding abilities of PDMS and Si wafer toward EglA were significantly higher than those of the other supporting materials. The optimized temperature and pH conditions for EglA immobilized on PDMS and on Si wafer were further determined by a response surface methodology (RSM) combined with a central composite design (CCD). The results indicated that the optimum pH and temperature values as well as the specific ß-glucanase activity of EglA on PDMS were higher than those of free-form EglA. In addition, EglA immobilized on PDMS could be reused up to six times with detectable enzyme activity, while the enzyme activity of Eg1A on Si wafer was undetectable after three cycles of enzyme reaction. The results demonstrate that PDMS is an attractive supporting material for EglA immobilization and could be developed into an enzyme chip or enzyme tube for potential industrial applications.
[Mh] Termos MeSH primário: Celulase/química
Celulase/metabolismo
Dimetilpolisiloxanos/química
Enzimas Imobilizadas/metabolismo
Piromyces/enzimologia
[Mh] Termos MeSH secundário: Celulase/genética
Celulase/isolamento & purificação
Enzimas Imobilizadas/química
Concentração de Íons de Hidrogênio
Modelos Teóricos
Análise de Regressão
Silício/química
Propriedades de Superfície
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dimethylpolysiloxanes); 0 (Enzymes, Immobilized); 63148-62-9 (baysilon); EC 3.2.1.4 (Cellulase); Z4152N8IUI (Silicon)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:140809
[Lr] Data última revisão:
140809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140328
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2014.887579


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[PMID]:22921355
[Au] Autor:Zhou H; Cheng JS; Wang BL; Fink GR; Stephanopoulos G
[Ad] Endereço:Department of Chemical Engineering, Massachusetts Institute of Technology, Room 56-469, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
[Ti] Título:Xylose isomerase overexpression along with engineering of the pentose phosphate pathway and evolutionary engineering enable rapid xylose utilization and ethanol production by Saccharomyces cerevisiae.
[So] Source:Metab Eng;14(6):611-22, 2012 Nov.
[Is] ISSN:1096-7184
[Cp] País de publicação:Belgium
[La] Idioma:eng
[Ab] Resumo:Xylose is the main pentose and second most abundant sugar in lignocellulosic feedstocks. To improve xylose utilization, necessary for the cost-effective bioconversion of lignocellulose, several metabolic engineering approaches have been employed in the yeast Saccharomyces cerevisiae. In this study, we describe the rational metabolic engineering of a S. cerevisiae strain, including overexpression of the Piromyces xylose isomerase gene (XYLA), Pichia stipitis xylulose kinase (XYL3) and genes of the non-oxidative pentose phosphate pathway (PPP). This engineered strain (H131-A3) was used to initialize a three-stage process of evolutionary engineering, through first aerobic and anaerobic sequential batch cultivation followed by growth in a xylose-limited chemostat. The evolved strain H131-A3-AL(CS) displayed significantly increased anaerobic growth rate (0.203±0.006 h⁻¹) and xylose consumption rate (1.866 g g⁻¹ h⁻¹) along with high ethanol conversion yield (0.41 g/g). These figures exceed by a significant margin any other performance metrics on xylose utilization and ethanol production by S. cerevisiae reported to-date. Further inverse metabolic engineering based on functional complementation suggested that efficient xylose assimilation is attributed, in part, to the elevated expression level of xylose isomerase, which was accomplished through the multiple-copy integration of XYLA in the chromosome of the evolved strain.
[Mh] Termos MeSH primário: Aldose-Cetose Isomerases/metabolismo
Etanol/metabolismo
Via de Pentose Fosfato/genética
Engenharia de Proteínas/métodos
Saccharomyces cerevisiae/fisiologia
Xilose/metabolismo
[Mh] Termos MeSH secundário: Aldose-Cetose Isomerases/genética
Evolução Molecular Direcionada/métodos
Etanol/isolamento & purificação
Melhoramento Genético/métodos
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Pichia/fisiologia
Piromyces/fisiologia
Regulação para Cima/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
3K9958V90M (Ethanol); A1TA934AKO (Xylose); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.17 (xylulokinase); EC 5.3.1.- (Aldose-Ketose Isomerases); EC 5.3.1.5 (xylose isomerase)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120828
[St] Status:MEDLINE


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[PMID]:22102024
[Au] Autor:Tseng CW; Ko TP; Guo RT; Huang JW; Wang HC; Huang CH; Cheng YS; Wang AH; Liu JR
[Ad] Endereço:Institute of Biotechnology, National Taiwan University, Taipei 10617, Taiwan.
[Ti] Título:Substrate binding of a GH5 endoglucanase from the ruminal fungus Piromyces rhizinflata.
[So] Source:Acta Crystallogr Sect F Struct Biol Cryst Commun;67(Pt 10):1189-94, 2011 Oct 01.
[Is] ISSN:1744-3091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The endoglucanase EglA from Piromyces rhizinflata found in cattle stomach belongs to the GH5 family of glycoside hydrolases. The crystal structure of the catalytic domain of EglA shows the (ß/α)(8)-barrel fold typical of GH5 enzymes. Adjacent to the active site of EglA, a loop containing a disulfide bond not found in other similar structures may participate in substrate binding. Because the active site was blocked by the N-terminal His tag of a neighbouring protein molecule in the crystal, enzyme-substrate complexes could not be obtained by soaking but were prepared by cocrystallization. The E154A mutant structure with a cellotriose bound to the -3, -2 and -1 subsites shows an extensive hydrogen-bonding network between the enzyme and the substrate, along with a stacking interaction between Trp44 and the -3 sugar. A possible dimer was observed in the crystal structure, but retention of activity in the E242A mutant suggested that the enzyme probably does not function as a dimer in solution. On the other hand, the first 100 amino acids encoded by the original cDNA fragment are very similar to those in the last third of the (ß/α)(8)-barrel fold, indicating that EglA comprises at least two catalytic domains acting in tandem.
[Mh] Termos MeSH primário: Celulase/química
Piromyces/enzimologia
Domínios e Motivos de Interação entre Proteínas
[Mh] Termos MeSH secundário: Celulase/genética
Celulase/metabolismo
Cristalografia por Raios X
Modelos Moleculares
Mutação
Estrutura Quaternária de Proteína
Homologia Estrutural de Proteína
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1202
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111122
[St] Status:MEDLINE
[do] DOI:10.1107/S1744309111032428


  9 / 49 MEDLINE  
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[PMID]:21306947
[Au] Autor:Chu CY; Tseng CW; Yueh PY; Duan CH; Liu JR
[Ad] Endereço:Institute of Biotechnology, National Taiwan University, Taipei, Taiwan.
[Ti] Título:Molecular cloning and characterization of a ß-glucanase from Piromyces rhizinflatus.
[So] Source:J Biosci Bioeng;111(5):541-6, 2011 May.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Cellulose is the most abundant renewable polysaccharide with a high potential for degradation to useful end products. In nature, most cellulose is produced as crystalline cellulose. Therefore, cellulases with high hydrolytic activity against crystalline cellulose are of great interest. In this study, a crystalline cellulose degradation enzyme was investigated. The cDNA encoding a ß-glucanase, CbhYW23-2, was cloned from the ruminal fungus Piromyces rhizinflatus. To examine the enzyme activities, CbhYW23-2 was expressed in Escherichia coli as a recombinant His(6) fusion protein and purified by immobilized metal ion-affinity chromatography. Response surface modeling (RSM) combined with central composite design (CCD) and regression analysis was then employed for the planned statistical optimization of the ß-glucanase activities of CbhYW23-2. The optimal conditions for the highest ß-glucanase activity of CbhYW23-2 were observed at 46.4°C and pH 6.0. The results suggested that RSM combined with CCD and regression analysis were effective in determining optimized temperature and pH conditions for the enzyme activity of CbhYW23-2. CbhYW23-2 also showed hydrolytic activities toward Avicel, carboxymethyl cellulose (CMC), lichenan, and pachyman. The results also proved that the high activity of CbhYW23-2 on crystalline cellulose makes it a promising candidate enzyme for biotechnological and industrial applications.
[Mh] Termos MeSH primário: Celulases/metabolismo
Proteínas Fúngicas/metabolismo
Glucanos/metabolismo
Piromyces/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Celulases/genética
Celulose/metabolismo
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas Fúngicas/genética
Concentração de Íons de Hidrogênio
Hidrólise
Dados de Sequência Molecular
Piromyces/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Especificidade por Substrato
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Glucans); 0 (Recombinant Proteins); 9004-34-6 (Cellulose); EC 3.2.1.- (Cellulases)
[Em] Mês de entrada:1108
[Cu] Atualização por classe:110419
[Lr] Data última revisão:
110419
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110211
[St] Status:MEDLINE
[do] DOI:10.1016/j.jbiosc.2011.01.009


  10 / 49 MEDLINE  
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[PMID]:21840805
[Au] Autor:Saxena S; Sehgal JP; Puniya AK; Singh K
[Ad] Endereço:Dairy Cattle Nutrition Division, National Dairy Research Institute, Karnal, Haryana, India.
[Ti] Título:Effect of administration of rumen fungi on production performance of lactating buffaloes.
[So] Source:Benef Microbes;1(2):183-8, 2010 Jun.
[Is] ISSN:1876-2891
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Anaerobic fungi were orally dosed to lactating buffaloes to study their effect on the digestibility of a diet (composed of 50% wheat straw and 50% concentrate along with six kg maize green/animal/day), rumen fermentation patterns and milk production. Group I (control) was administered with fungus-free anaerobic broth, while group II and III were administered with Orpinomyces sp. C-14 or Piromyces sp. WNG-12 (250 ml; 3-5 days of growth/animal/ week), respectively. Milk production was higher in group II and III (8.42 and 8.48 kg/d) than in the control (8.03 kg/d) with virtually the same feed intake (i.e. 11.50 and 10.62 and 11.79 kg, respectively). There was an increase of 6% fat-corrected milk yield/animal/day in group II and III, respectively compared to the control. The milk fat was higher in the fungal culture administered groups than in the control group. The digestibility of dry matter, crude protein, neutral detergent fibre, acid detergent fibre, cellulose and digestible energy also increased significantly in group II and III. The pH and ammonia nitrogen were lower, whereas total volatile fatty acids, total nitrogen, trichloroacid precipitable nitrogen and number of zoospores/ml of rumen liquor were higher in group II and III when compared to the control. Hence, it can be stated that rumen fungi can be used as a direct-fed microbial in lactating buffaloes, to enhance the digestibility of wheat straw based diets leading to higher production.
[Mh] Termos MeSH primário: Dieta/métodos
Lactação
Neocallimastigales/crescimento & desenvolvimento
Piromyces/crescimento & desenvolvimento
Rúmen/microbiologia
[Mh] Termos MeSH secundário: Animais
Búfalos
Feminino
Leite/química
Leite/secreção
Triticum
Zea mays
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1112
[Cu] Atualização por classe:110815
[Lr] Data última revisão:
110815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110816
[St] Status:MEDLINE
[do] DOI:10.3920/BM2009.0018



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