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| Registros recuperados: 12 | |
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| Fawzi,Eman Mohamed. |
| Thirty fungal species grown on Cichorium intybus L. root extract as a sole carbon source, were screened for the production of exo-inulinase activities. The thermophile Thielavia terrestris NRRL 8126 and mesophile Aspergillus foetidus NRRL 337 gave the highest production levels of inulinases I & II at 50 and 24 ºC respectively. Yeast extract and peptone were the best nitrogen sources for highest production of inulinases I & II at five and seven days of incubation respectively. The two inulinases I & II were purified to homogeneity by gel-filtration and ion-exchange chromatography with 66.0 and 42.0 fold of purification respectively. The optimum temperatures of purified inulinases I & II were 75 and 50 ºC respectively.... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Inulinases; Production; Purification; Thermophile; Thermostability. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000200028 |
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| Ribeiro,Liliane Fraga Costa; Vaz,Marcelo Gomes Marçal Vieira; Chaves-Alves,Virgínia Maria; Vanetti,Maria Cristina Dantas; Kasuya,Maria Catarina Megumi; Passos,Flávia Maria Lopes; Nascimento,Antônio Galvão do. |
| Xylanolytic enzymes produced by Lentinula edodes UFV70, cultivated in eucalyptus sawdust/rice bran medium, were stable at 50, 60 and 65ºC for 21 hours, losing only 15-25% activity. Fungus incubation at 50ºC for 12 hours and at 65ºC for 24 hours increased the amount of xylose produced. |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Xylanase; Thermostability; Lentinula edodes; Xylose. |
| Ano: 2012 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000100021 |
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| Kansal,Rekha; Kumar,Mukesh; Kuhar,Kalika; Gupta,Ram N.; Subrahmanyam,Bhattiprolu; Koundal,Kirpa R.; Gupta,Vijay K.. |
| Protease inhibitors in legumes are one of the most promising weapons that confer resistance against insects by inhibiting proteases present in the gut of insect larvae. In the present study, trypsin inhibitor activity was detected in the seed flour extracts of 10 selected varieties of chickpea. The presence of inhibitor was confirmed by dot blot analysis. All the varieties showed inhibitory activity in vitro against the gut protease of Helicoverpa armigera (HGP). Trypsin inhibitor has been purified to near homogeneity to 60.46 fold and 29.20% recovery from chickpea seeds using heat denaturation, ammonium sulphate fractionation, DEAE-Sephadex A-25 and Sephadex G-75. The purified inhibitor showed a single band on SDS-PAGE corresponding to molecular mass of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Chickpea; Dot blot; Insect bioassay; PH stability; Thermostability. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202008000400007 |
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| Oliveira,Rodrigo de Queiroz; Valasques Junior,Gildomar Lima; Uetanabaro,Ana Paula Trovatti; Koblitz,Maria Gabriela Bello; Góes-Neto,Aristóteles; Rosa,Carlos Augusto; Assis,Sandra Aparecida de. |
| Microbial pectinolytic enzymes are known to play a commercially important role in a number of industrial processes. Two kinds of yeast can be discerned regarding the production of enzymes. One group includes those which can produce enzymes in the absence of an inducer, and the other group comprises the yeasts that produce enzymes in the presence of an inducer. The objective of this study was to investigate the influence of pectic substances, glucose, pH, and temperature on the polygalacturonase activity by Kluyveromyces marxianus CCMB 322. The yeast was grown in a fermentation broth containing different concentrations of glucose and pectic substances. The polygalacturonase activity was determined by the DNS method, and the pH and temperature were optimized... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Yeasts; Enzymes; Thermostability; Pectic substances; Biotechnology. |
| Ano: 2012 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612012000300012 |
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| Rudrappa,Thimmaraju; Neelwarne,Bhagyalakshmi; Kumar,Vinod; Lakshmanan,Venkatachalam; Venkataramareddy,Sreedhar Reddampalli; Aswathanarayana,Ravishankar Gokare. |
| The genetically transformed roots of red beet have been shown, for the first time, to produce very high levels of peroxidase (POD; EC 1.11.1.7) accounting for 1.21 x 10(6) Units L-1. Of the ten clones established using different strains of Agrobacterium rhizogenes, one was that from the strain LMG-150, three each from A 2/83, A 20/83 and A4. All the clones showed true integration of T-DNA when tested by PCR and Southern hybridization methods. Each clone differed significantly from the others in growth, hormone dependency and POD production where LMG-150 produced highest biomass (140 g FW L-1) as well as POD (ranging from 8000-9000 U g-1 FW and 1.18 x 10(6) U L-1 with a specific activity of 600 U mg-1 protein) on hormone-free medium, both in shake-flask as... |
| Tipo: Journal article |
Palavras-chave: Agrobacterium rhizogenes; Auxins; Elicitation; T-DNA; Thermostability; Transformation. |
| Ano: 2005 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582005000200008 |
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| Nawani,Neerupma; Singh,Rajvinder; Kaur,Jagdeep. |
| A thermostable lipase was partially purified from the culture supernatant of a thermophilic Bacillus sp. The enzyme is optimally active at 60ºC and pH 8.0. The enzyme showed enhancement in activity in presence of benzene or hexane (30% v/v each). The activity (assayed by determining the release of pNP from pNP laurate) was stimulated up to 60% of these solvents in enzyme reaction mixture. The catalytic properties of this thermostable enzyme can be further improved via the use of different immobilization techniques and reaction conditions. Enzyme was immobilized on different solid supports and their enzyme activity and stability was compared. The enzyme was adsorbed on silica and HP-20 beads followed by cross-linking with gluteraldehyde on HP-20,... |
| Tipo: Journal article |
Palavras-chave: Esterification; Immobilization; Lipase; Thermostability. |
| Ano: 2006 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000500011 |
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| Quiroga,Evelina; Priolo,Nora; Marchese,José; Barberis,Sonia. |
| In this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,N-dimethylformamide, acetophenone, diethyl ether, methanol, ethylene glycol and toluene) with low and constant water content on substrate preferences, thermostability and stability (caseinolytic activity retention after 4 h) of proteases of Araujia hortorum Fourn. (Asclepiadaceae). The stability of araujiain was high in N,N-dimethylformamide and ethanol at 40ºC, but decreased at higher temperature. Araujiain substrates preferences in buffer Tris-HCl (pH 8), ethylene glycol and N,N-dimethylformamide exhibited different patterns, but the... |
| Tipo: Journal article |
Palavras-chave: Araujia hortorum Fourn; Organic solvents; Plant protease; Substrate preferences; Thermostability. |
| Ano: 2006 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000100004 |
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| Castrec, Benoit. |
| DNA replication is a functionally conserved mechanism among the three domains of life. This processus is performed by DNA polymerases with two accessories factors, PCNA and RF-C, sliding clamp and clamp loader, respectively. Our model of study, the Euryarchaeota Pyrococcus abyssi, possesses one monomeric DNA polymerase, belonging to the Family B, and one heterodimeric DNA polymerase, belonging to the Family D. Usually, proteins interact with PCNA at a hydrophobic pocket which is formed by the IDCL (interdomain connecting loop) and the C-terminus. These interactions are mediated through common motifs like the PIP box (motif PCNA interacting Protein). We have demonstrated that Pol B has just one PIP box motif at the C-terminus, while Pol D has two PIP-type... |
| Tipo: Text |
Palavras-chave: Thermostability; Interactions; Motifs; DNA replication; RF C; PCNA; DNA polymerases; Archaea; Thermostabilité; Interactions; Motifs; Réplication de l'ADN; RF C; PCNA; ADN polymérases; Archaea. |
| Ano: 2009 |
URL: http://archimer.ifremer.fr/doc/2009/these-6940.pdf |
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| FRANCO,OCTÁVIO LUIZ; GONDIM,LORRANCE ABREU; BEZERRA,KÁTIA REGINA; GUERRA,MARIA ELANE DE CARVALHO; LIMA,CARMEM ROGÉLIA FARIAS MACHADO; ENÉAS-FILHO,JOAQUIM; PRISCO,JOSÉ TARQUÍNIO; GOMES-FILHO,ENÉAS. |
| Partial purification and characterization of ribonucleases (RNase; EC 3.1.27.1) present in roots, stem and leaves of 5 day-old Pitiúba cowpea [Vigna unguiculata (L.) Walp.] seedlings are described. Crude extracts from the different tissues were precipitated with ammonium sulfate followed by ionic exchange chromatography (CM-Cellulose) resulting in purification factors of 48-fold for roots, 21 for stem and 42 for leaves. No deoxyribonuclease activity was practically observed. The molecular masses of the RNases did not significantly differ, averaging 16.3 kDa. Leaf RNase was stable up to 50ºC while the others were inactivated at this temperature. The maximal inactivation for both stem and roots RNases was reached at 70ºC while for leaf it occurred at 80ºC.... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Enzyme effectors; Molecular mass; Nuclease; Optimum pH; Seedlings; Thermostability; Vigna unguiculata. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-31312001000300010 |
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| Registros recuperados: 12 | |
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