844 research outputs found

    Differences in the Volatile Profile of Apple Cider Fermented with Schizosaccharomyces pombe and Schizosaccharomyces japonicus

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    In this study, two strains of Schizosaccharomyces pombe (NCAIM Y01474(T) and SBPS) and two strains of Schizosaccharomyces japonicus (DBVPG 6274(T), M23B) were investigated for their capacity to ferment apple juice and influence the volatile compounds of cider compared to Saccharomyces cerevisiae EC1118. The ethanol tolerance and deacidification capacity of Schizosaccharomyces yeasts could make them potential substitutes for the commonly used S. cerevisiae starter cultures. Despite different time courses (10-30 d), all strains could complete the fermentation process, and Schizosaccharomyces strains reduced the concentration of malic acid in the apple juice. Results indicated that each yeast exerted a distinctive impact on the volatile profile of the apple cider, giving final products separated using a principal component analysis. The volatile composition of the cider exhibited significant differences in the concentration of alcohols, esters, and fatty acids. Particularly, the flocculant strain S. japonicus M23B increased the levels of ethyl acetate (315.44 +/- 73.07 mg/L), isoamyl acetate (5.99 +/- 0.13 mg/L), and isoamyl alcohol (24.77 +/- 15.19 mg/L), while DBVPG 6274(T) incremented the levels of phenyl ethyl alcohol and methionol up to 6.19 +/- 0.51 mg/L and 3.72 +/- 0.71 mg/L, respectively. A large production of terpenes and ethyl esters (e.g., ethyl octanoate) was detected in the cider fermented by S. cerevisiae EC1118. This study demonstrates, for the first time, the possible application of S. japonicus in cider-making to provide products with distinctive aromatic notes"

    Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras.

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    The troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114137

    Effects of phase separation on the magnetization, x-ray diffraction, and Raman scattering of (La1-yNdy)(1-x)CaxMnO3 (y=0,0.5,1.0; x=1/3)

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    Dc-magnetization, x-ray diffraction, and Raman-scattering studies in polycrystalline (La1-yNdy)(t-x)CaxMnO3 (y = 0.0,0.5,1.0, and x = 1/3) samples are presented. The samples with y = 0.5 and 1.0 show complex magnetic states at low temperatures, with a ferromagnetic coupling strength that weal;ens with increasing y. X-ray measurements show a single crystallographic phase at all temperatures for y = 0.5, with lattice parameter anomalies at temperatures related to electronic and magnetic transitions. The presence of high-frequency vibrational modes in Raman-scattering measurements indicates the existence of charge- and orbital-ordered domains for y=0.5 and 1.0, which are closely related to the antiferromagnetic component identified by the magnetization experiments. The close relationship between results obtained by magnetic, structural, and optical probes is discussed.63

    Effects Of Phase Separation On The Magnetization, X-ray Diffraction, And Raman Scattering Of (la1-yndy) 1-xcaxmno3 (y = 0,0.5,1.0;x = 1/3)

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    Dc-magnetization, x-ray diffraction, and Raman-scattering studies in polycrystalline (La1-yNdy)1-xCaxMnO3 (y = 0.0,0.5,1.0, and x = 1/3) samples are presented. The samples with y = 0.5 and 1.0 show complex magnetic states at low temperatures, with a ferromagnetic coupling strength that weakens with increasing y. X-ray measurements show a single crystallographic phase at all temperatures for y=0.5, with lattice parameter anomalies at temperatures related to electronic and magnetic transitions. The presence of high-frequency vibrational modes in Raman-scattering measurements indicates the existence of charge- and orbital-ordered domains for y = 0.5 and 1.0, which are closely related to the antiferromagnetic component identified by the magnetization experiments. The close relationship between results obtained by magnetic, structural, and optical probes is discussed.636644041644046Wollan, E.O., Koehler, W.C., (1955) Phys. Rev., 100, p. 545Goodenough, J.B., (1955) Phys. Rev., 100, p. 564Chen, C.H., Cheong, S.-W., (1996) Phys. Rev. Lett., 76, p. 4042Radaelli, P.G., Cox, D.E., Marezio, M., Cheong, S.-W., Schiffer, P.E., Ramirez, A.P., (1995) Phys. Rev. Lett., 75, p. 4488Hwang, H.Y., Cheong, S.-W., Radaelli, P.G., Marezio, M., Batlogg, B., (1995) Phys. Rev. Lett., 75, p. 914Coey, J.M.D., Viret, M., Ranno, L., Ounadjela, K., (1995) Phys. Rev. Lett., 75, p. 3910Uehara, M., Mori, S., Chen, C.H., Cheong, S.-W., (1999) Nature (London), 399, p. 560Moreo, A., Yunoke, S., Dagotto, E., (1999) Science, 283, p. 2034. , and references thereinArchibald, W., Zhou, J.-S., Goodenough, J.B., (1996) Phys. Rev. B, 53, p. 14445Zhou, J.-S., Archibald, W., Goodenough, J.B., (1996) Nature (London), 381, p. 770Rao, G.H., Sun, J.R., Liang, J.K., Zhou, W.Y., Cheng, X.R., (1996) Appl. Phys. Lett., 69, p. 424Rao, G.H., Sun, J.R., Liang, J.K., Zhou, W.Y., (1997) Phys. Rev. B, 55, p. 3742Zhou, J.-S., Goodenough, J.B., (1998) Phys. Rev. Lett., 80, p. 2665Ibarra, M.R., Zhao, G.-M., De Teresa, J.M., García-Landa, B., Arnold, Z., Marquina, C., Algarabel, P.A., Ritter, C., (1998) Phys. Rev. B, 57, p. 7446Baszynski, J., Kovac, J., Kowalczyk, A., (1999) J. Magn. Magn. Mater., 195, p. 93Moritomo, Y., (1999) Phys. Rev. B, 60, p. 10374Young, R.A., Sakthivel, A., Moss, T.S., Paiva-Santos, C.O., (1995) J. Appl. Crystallogr., 28, p. 366Radaelli, P.G., Cox, D.E., Marezio, M., Cheong, S.-W., (1997) Phys. Rev. B, 55, p. 3015Huang, Q., Santoro, A., Lynn, J.W., Erwin, R.W., Borches, J.A., Peng, J.L., Ghosh, K., Greene, R.L., (1998) Phys. Rev. B, 58, p. 2684Irwin, J.C., Chrzanowski, J., Franck, J.P., (1999) Phys. Rev. B, 59, p. 9362Abrashev, M.V., Ivanov, V.G., Iliev, M.N., Chakalov, R.A., Chakalova, R.I., Thomsen, C., (1999) Phys. Status Solidi B, 215, p. 631Liarokapis, E., Leventouri, Th., Lampakis, D., Palles, D., Neumeier, J.J., Goodwin, D.H., (1999) Phys. Rev. B, 60, p. 12758Granado, E., Moreno, N.O., García, A., Sanjurjo, J.A., Rettori, C., Torriani, I., Oseroff, S.B., Tokura, Y., (1998) Phys. Rev. B, 58, p. 11435Yoon, S., Liu, H.L., Schollerer, G., Cooper, S.L., Han, P.D., Payne, D.A., Cheong, S.-W., Fisk, Z., (1998) Phys. Rev. B, 58, p. 2795Liu, H.L., Yoon, S., Cooper, S.L., Cheong, S.-W., Han, P.D., Payne, D.A., (1998) Phys. Rev. B, 58, pp. R10115Liu, K., Wu, X.W., Ahn, K.H., Sulchek, T., Chien, C.L., Xiao, J.Q., (1996) Phys. Rev. B, 54, p. 3007Granado, E., Pagliuso, P.G., Sanjurjo, J.A., Rettori, C., Oseroff, S.B., Causa, M.T., Butera, A., Schultz, S., (1998) Non-Crystalline and Nanoscale Materials, pp. 105-115. , edited by J. Rivas and M.A. López-Quintela (World Scientific, Singapore)Granado, E., Sanjurjo, J.A., Rettori, C., Prado, F., Sánchez, R.D., Caneiro, A., Oseroff, S.B., (2000) Phys. Status Solidi B, 220, p. 609Dediu, V., Ferdeghini, C., Matacotta, F.C., Nozar, P., Ruani, G., (2000) Phys. Rev. Lett., 84, p. 4489Adams, C.P., Lynn, J.W., Mukovskii, Y.M., Arsenov, A.A., Shulyatev, D.A., (2000) Phys. Rev. Lett., 85, p. 3954Dai, P., Fernandez-Baca, J.A., Wakabayashi, N., Plummer, E.W., Tomioka, Y., Tokura, Y., (2000) Phys. Rev. Lett., 85, p. 255

    Design of ideal vibrational signals for stinkbug male attraction through vibrotaxis experiments

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    Many groups of insects utilize substrate-borne vibrations for intraspecific communication. This characteristic makes them a suitable model for exploring the vibrations as a tool for pest control in alternative to chemicals. The detailed knowledge of the species communication is a prerequisite to select the best signals to use. In this sense, this study aimed at exploring the use of substrate-borne vibrations for pest control of the brown marmorated stink bug (BMSB), Halyomorpha halys Stål (Heteroptera: Pentatomidae). To this purpose, in a first set of experiments, we identified the spectral and temporal characteristics that best elicit male responsiveness. Bioassays were conducted with artificial signals that mimicked the natural female calling signal. In a second part, we used the acquired knowledge to synthesize new signals endowed with different degrees of attractiveness in single and two choice bioassays using a wooden custom-made T stand

    The genome of Bifidobacterium pseudocatenulatum IPLA 36007, a human intestinal strain with isoflavone-activation activity

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    Background: Bifidobacterium species, including Bifidobacterium pseudocatenulatum, are among the dominant microbial populations of the human gastrointestinal tract. They are also major components of many commercial probiotic products. Resident and transient bifidobacteria are thought to have several beneficial health effects. However, our knowledge of how these bacteria interact and communicate with host cells remains poor. This knowledge is essential for scientific support of their purported health benefits and their rational inclusion in functional foods. Results: This work describes the draft genome sequence of Bifidobacterium pseudocatenulatum IPLA 36007, a strain isolated as dominant from the feces of a healthy human. Besides several properties of probiosis, IPLA 36007 exhibited the capability of releasing aglycones from soy isoflavone glycosides. The genome contains 1,851 predicted genes, including 54 genes for tRNAs and fie copies of unique 16S, 23S and 5S rRNA genes. As key attributes of the IPLA 36007 genome we can mention the presence of a lysogenic phage, a cluster encoding type IV fimbriae, and a locus encoding a clustered, regularly interspaced, short, palindromic repeat (CRISPR)-Cas system. Four open reading frames (orfs) encoding \u3b2-glucosidases belonging to the glycosyl hydrolase family 3, which may act on isoflavone glycosides, were encountered. Additionally, one gene was found to code for a glycosyl hydrolase of family 1 that might also have \u3b2-glucosidase activity. Conclusion: The availability of the B. pseudocatenulatum IPLA 36007 genome should allow the enzyme system involved in the release of soy isoflavone aglycones from isoflavone glycosides, and the molecular mechanisms underlying the strain's probiotic properties, to be more easily understood
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