The Experts below are selected from a list of 5109861 Experts worldwide ranked by ideXlab platform
Yasunori Tanji - One of the best experts on this subject based on the ideXlab platform.
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bacillus amyloliquefaciens phage endolysin can enhance permeability of pseudomonas aeruginosa outer membrane and induce cell lysis
Applied Microbiology and Biotechnology, 2004Co-Authors: Yuji Orito, Masatomo Morita, Katsutoshi Hori, Hajime Unno, Yasunori TanjiAbstract:To determine the function of the C-terminal region of Bacillus amyloliquefaciens phage endolysin on Pseudomonas aeruginosa lysis, the permeabilization of the outer membrane of P. aeruginosa was analyzed. Glu-15 to His (E15H) and Thr-32 to Glu (T32E) substitutions were introduced into the Bacillus phage endolysin. Neither E15H nor T32E substitution induced enzymatic and antibacterial activities. These two, Glu-15 and Thr-32, were considered to be the active center of the enzyme. The addition of purified E15H and T32E proteins to P. aeruginosa cells induced the release of periplasmic β-lactamase from the cells, indicating that both proteins enhance permeabilization of the outer membrane. However, the addition of E15H and T32E proteins to P. aeruginosa cells did not induce the release of cytoplasmic ATP from the cells. These results indicate that the antibacterial activity of the endolysin requires both the C-terminal enhancement of the permeabilization of the P. aeruginosa outer membrane and N-terminal enzymatic activity.
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bacillus amyloliquefaciens phage endolysin can enhance permeability of pseudomonas aeruginosa outer membrane and induce cell lysis
Applied Microbiology and Biotechnology, 2004Co-Authors: Yuji Orito, Masatomo Morita, Katsutoshi Hori, Hajime Unno, Yasunori TanjiAbstract:To determine the function of the C-terminal region of Bacillus amyloliquefaciens phage endolysin on Pseudomonas aeruginosa lysis, the permeabilization of the outer membrane of P. aeruginosa was analyzed. Glu-15 to His (E15H) and Thr-32 to Glu (T32E) substitutions were introduced into the Bacillus phage endolysin. Neither E15H nor T32E substitution induced enzymatic and antibacterial activities. These two, Glu-15 and Thr-32, were considered to be the active center of the enzyme. The addition of purified E15H and T32E proteins to P. aeruginosa cells induced the release of periplasmic beta-lactamase from the cells, indicating that both proteins enhance permeabilization of the outer membrane. However, the addition of E15H and T32E proteins to P. aeruginosa cells did not induce the release of cytoplasmic ATP from the cells. These results indicate that the antibacterial activity of the endolysin requires both the C-terminal enhancement of the permeabilization of the P. aeruginosa outer membrane and N-terminal enzymatic activity.
Sadaaki Iwanaga - One of the best experts on this subject based on the ideXlab platform.
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cdna cloning and deduced amino acid sequence of prothrombin activator ecarin from kenyan echis carinatus venom
Biochemistry, 1995Co-Authors: S. Nishida, Taizo Fujita, Noriatsu Kohno, Isao J Kido, Hideko Atoda, Mark J. I. Paine, Shunichiro Kawabata, Hiroyuki Takeya, Takashi Morita, Sadaaki IwanagaAbstract:The complete amino acid sequence of ecarin is deduced from the nucleotide sequence of a cDNA clone isolated by screening a venomous gland cDNA library of Kenyan Echis carinatus. The cDNA sequence with 2379 base pairs encodes an open reading frame of 616 amino acids with a remarkable sequence homology to the putative precursor protein of trigramin from Trimeresurus gramineus venom (61% identity) and a large hemorrhagin, jararhagin, from the pit viper Bothrops jararaca venom (62% identity). Thus, ecarin, as well as jararhagin and trigramin, is translated as a precursor protein, which may be processed posttranslationally. The ecarin proprotein has a "cysteine switch" motif (-Pro-Lys-Met-Cys-Gly-Val-) similar to that involved in the activation of matrix metalloproteinase zymogens. The processed mature protein consists of 426 amino acid residues (residues 191-616), showing the strongest sequence similarity with that of Russell's viper venom factor X activator (RVV-X) heavy chain (64% identity). Like RVV-X heavy chain, ecarin contains metalloproteinase, disintegrin, and cysteine-rich domains. The metalloproteinase domain has a typical zinc-chelating sequence (-His-Glu-Xaa-Xaa-His-Xaa-Xaa-Gly-Xaa-Xaa-His-), as found in crayfish astacin. In the disintegrin domain of ecarin, the Arg-Gly-Asp sequence is replaced by Arg-Asp-Asp, as found in the disintegrin domains of RVV-X heavy chain (Arg-Asp-Glu) and a guinea pig sperm fusion protein, PH-30 beta (Thr-Asp-Glu). These findings show that while there are structural and evolutionary relationships among these proteins, each has a unique functional activity.
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cdna cloning and deduced amino acid sequence of prothrombin activator ecarin from kenyan echis carinatus venom
Biochemistry, 1995Co-Authors: S. Nishida, Taizo Fujita, Noriatsu Kohno, Isao J Kido, Hideko Atoda, Mark J. I. Paine, Shunichiro Kawabata, Hiroyuki Takeya, Takashi Morita, Sadaaki IwanagaAbstract:The complete amino acid sequence of ecarin is deduced from the nucleotide sequence of a cDNA clone isolated by screening a venomous gland cDNA library of Kenyan Echis curinurus. The cDNA sequence with 2379 base pairs encodes an open reading frame of 616 amino acids with a remarkable sequence homology to the putative precursor protein of trigramin from Trimeresurus grumineus venom (61% identity) and a large hemorrhagin, jararhagin, from the pit viper Bothrops jururucu venom (62% identity). Thus, ecarin, as well as jararhagin and trigramin, is translated as a precursor protein, which may be processed posttranslationally. The ecarin proprotein has a "cysteine switch" motif (-Pro-Lys- Met-Cys-Gly-Val-) similar to that involved in the activation of matrix metalloproteinase zymogens. The processed mature protein consists of 426 amino acid residues (residues 191 -616), showing the strongest sequence similarity with that of Russell's viper venom factor X activator (RVV-X) heavy chain (64% identity). Like RVV-X heavy chain, ecarin contains metalloproteinase, disintegrin, and cysteine-rich domains. The metalloproteinase domain has a typical zinc-chelating sequence (-His-Glu-Xaa-Xaa-His- Xaa-Xaa-Gly-Xga-Xaa-His-), as found in crayfish astacin. In the disintegrin domain of ecarin, the Arg- Gly-Asp sequence is replaced by Arg-Asp-Asp, as found in the disintegrin domains of RVV-X heavy chain (Arg-Asp-Glu) and a guinea pig sperm fusion protein, PH-30P (Thr-Asp-Glu). These findings show that while there are structural and evolutionary relationships among these proteins, each has a unique functional activity.
Thomas Hofmann - One of the best experts on this subject based on the ideXlab platform.
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Quantitation of Key Tastants and Re-engineering the Taste of Parmesan Cheese
Journal of agricultural and food chemistry, 2016Co-Authors: Hedda Hillmann, Thomas HofmannAbstract:Targeted quantitation of 65 candidate taste compounds and ranking on the basis of dose-over-threshold (DoT) factors, followed by taste re-engineering and omission experiments in aqueous solution as well as in a cheese-like model matrix, led to the identification of a total of 31 key tastants (amino acids, organic acids, fatty acids, biogenic amines, and minerals) with DoT factors ≥1.0 and a total of 15 subthreshold, but kokumi-enhancing, γ-glutamyl peptides in extraordinarily high concentrations of 20468 μmol/kg. Among the γ-glutamyl peptides, γ-Glu-Gly, γ-Glu-Ala, γ-Glu-Thr, γ-Glu-Asp, γ-Glu-Lys, γ-Glu-Glu, γ-Glu-Trp, γ-Glu-Gln, and γ-Glu-His have been identified for the first time in Parmesan cheese. The excellent match of the sensory profile of the taste recombinants and the authentic cheese demonstrated the identified taste compounds to be fully sufficient to create the characteristic taste profile of the Parmesan cheese. This molecular blueprint of a Parmesan’s chemosensory signature might be a usefu...
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A series of kokumi peptides impart the long-lasting mouthfulness of matured Gouda cheese.
Journal of agricultural and food chemistry, 2009Co-Authors: Simone Toelstede, Andreas Dunkel, Thomas HofmannAbstract:Comparative sensory analysis revealed that a 44-week-matured Gouda cheese (GC44) exhibited a much more pronounced mouthfulness and long-lasting taste complexity when compared to a young Gouda cheese ripened for only 4 weeks (GC4). To identify the molecules underlying that so-called kokumi sensation, a sensomics approach was applied on the water-soluble extract (WSE44) of GC44 by combining gel permeation chromatography (GPC) with analytical sensory tools. HPLC-MS/MS experiments on GPC fractions inducing a kokumi sensation when tasted in an aqueous biomimetic taste recombinant solution (rWSE44) enabled the identification of 8 alpha-L-glutamyl and 10 gamma-L-glutamyl dipeptides as candidate kokumi-enhancing molecules. Among those, only the gamma-L-glutamyl dipeptides were found to impart an enhanced kokumi sensation to the matured cheese, whereas none of the alpha-glutamyl peptides were found to be active. Among the gamma-L-glutamyl peptides, the candidates gamma-Glu-Glu, gamma-Glu-Gly, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Leu, and gamma-Glu-His, present in GC44 in concentrations between 4.11 and 17.66 micromol/kg, were identified for the first time as the key kokumi molecules enhancing mouthfulness and complex taste continuity of the matured cheese.
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a series of kokumi peptides impart the long lasting mouthfulness of matured gouda cheese
Journal of Agricultural and Food Chemistry, 2009Co-Authors: Simone Toelstede, Andreas Dunkel, Thomas HofmannAbstract:Comparative sensory analysis revealed that a 44-week-matured Gouda cheese (GC44) exhibited a much more pronounced mouthfulness and long-lasting taste complexity when compared to a young Gouda cheese ripened for only 4 weeks (GC4). To identify the molecules underlying that so-called kokumi sensation, a sensomics approach was applied on the water-soluble extract (WSE44) of GC44 by combining gel permeation chromatography (GPC) with analytical sensory tools. HPLC-MS/MS experiments on GPC fractions inducing a kokumi sensation when tasted in an aqueous biomimetic taste recombinant solution (rWSE44) enabled the identification of 8 α-l-glutamyl and 10 γ-l-glutamyl dipeptides as candidate kokumi-enhancing molecules. Among those, only the γ-l-glutamyl dipeptides were found to impart an enhanced kokumi sensation to the matured cheese, whereas none of the α-glutamyl peptides were found to be active. Among the γ-l-glutamyl peptides, the candidates γ-Glu-Glu, γ-Glu-Gly, γ-Glu-Gln, γ-Glu-Met, γ-Glu-Leu, and γ-Glu-His, p...
Yuji Orito - One of the best experts on this subject based on the ideXlab platform.
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bacillus amyloliquefaciens phage endolysin can enhance permeability of pseudomonas aeruginosa outer membrane and induce cell lysis
Applied Microbiology and Biotechnology, 2004Co-Authors: Yuji Orito, Masatomo Morita, Katsutoshi Hori, Hajime Unno, Yasunori TanjiAbstract:To determine the function of the C-terminal region of Bacillus amyloliquefaciens phage endolysin on Pseudomonas aeruginosa lysis, the permeabilization of the outer membrane of P. aeruginosa was analyzed. Glu-15 to His (E15H) and Thr-32 to Glu (T32E) substitutions were introduced into the Bacillus phage endolysin. Neither E15H nor T32E substitution induced enzymatic and antibacterial activities. These two, Glu-15 and Thr-32, were considered to be the active center of the enzyme. The addition of purified E15H and T32E proteins to P. aeruginosa cells induced the release of periplasmic β-lactamase from the cells, indicating that both proteins enhance permeabilization of the outer membrane. However, the addition of E15H and T32E proteins to P. aeruginosa cells did not induce the release of cytoplasmic ATP from the cells. These results indicate that the antibacterial activity of the endolysin requires both the C-terminal enhancement of the permeabilization of the P. aeruginosa outer membrane and N-terminal enzymatic activity.
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bacillus amyloliquefaciens phage endolysin can enhance permeability of pseudomonas aeruginosa outer membrane and induce cell lysis
Applied Microbiology and Biotechnology, 2004Co-Authors: Yuji Orito, Masatomo Morita, Katsutoshi Hori, Hajime Unno, Yasunori TanjiAbstract:To determine the function of the C-terminal region of Bacillus amyloliquefaciens phage endolysin on Pseudomonas aeruginosa lysis, the permeabilization of the outer membrane of P. aeruginosa was analyzed. Glu-15 to His (E15H) and Thr-32 to Glu (T32E) substitutions were introduced into the Bacillus phage endolysin. Neither E15H nor T32E substitution induced enzymatic and antibacterial activities. These two, Glu-15 and Thr-32, were considered to be the active center of the enzyme. The addition of purified E15H and T32E proteins to P. aeruginosa cells induced the release of periplasmic beta-lactamase from the cells, indicating that both proteins enhance permeabilization of the outer membrane. However, the addition of E15H and T32E proteins to P. aeruginosa cells did not induce the release of cytoplasmic ATP from the cells. These results indicate that the antibacterial activity of the endolysin requires both the C-terminal enhancement of the permeabilization of the P. aeruginosa outer membrane and N-terminal enzymatic activity.
S. Nishida - One of the best experts on this subject based on the ideXlab platform.
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cdna cloning and deduced amino acid sequence of prothrombin activator ecarin from kenyan echis carinatus venom
Biochemistry, 1995Co-Authors: S. Nishida, Taizo Fujita, Noriatsu Kohno, Isao J Kido, Hideko Atoda, Mark J. I. Paine, Shunichiro Kawabata, Hiroyuki Takeya, Takashi Morita, Sadaaki IwanagaAbstract:The complete amino acid sequence of ecarin is deduced from the nucleotide sequence of a cDNA clone isolated by screening a venomous gland cDNA library of Kenyan Echis carinatus. The cDNA sequence with 2379 base pairs encodes an open reading frame of 616 amino acids with a remarkable sequence homology to the putative precursor protein of trigramin from Trimeresurus gramineus venom (61% identity) and a large hemorrhagin, jararhagin, from the pit viper Bothrops jararaca venom (62% identity). Thus, ecarin, as well as jararhagin and trigramin, is translated as a precursor protein, which may be processed posttranslationally. The ecarin proprotein has a "cysteine switch" motif (-Pro-Lys-Met-Cys-Gly-Val-) similar to that involved in the activation of matrix metalloproteinase zymogens. The processed mature protein consists of 426 amino acid residues (residues 191-616), showing the strongest sequence similarity with that of Russell's viper venom factor X activator (RVV-X) heavy chain (64% identity). Like RVV-X heavy chain, ecarin contains metalloproteinase, disintegrin, and cysteine-rich domains. The metalloproteinase domain has a typical zinc-chelating sequence (-His-Glu-Xaa-Xaa-His-Xaa-Xaa-Gly-Xaa-Xaa-His-), as found in crayfish astacin. In the disintegrin domain of ecarin, the Arg-Gly-Asp sequence is replaced by Arg-Asp-Asp, as found in the disintegrin domains of RVV-X heavy chain (Arg-Asp-Glu) and a guinea pig sperm fusion protein, PH-30 beta (Thr-Asp-Glu). These findings show that while there are structural and evolutionary relationships among these proteins, each has a unique functional activity.
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cdna cloning and deduced amino acid sequence of prothrombin activator ecarin from kenyan echis carinatus venom
Biochemistry, 1995Co-Authors: S. Nishida, Taizo Fujita, Noriatsu Kohno, Isao J Kido, Hideko Atoda, Mark J. I. Paine, Shunichiro Kawabata, Hiroyuki Takeya, Takashi Morita, Sadaaki IwanagaAbstract:The complete amino acid sequence of ecarin is deduced from the nucleotide sequence of a cDNA clone isolated by screening a venomous gland cDNA library of Kenyan Echis curinurus. The cDNA sequence with 2379 base pairs encodes an open reading frame of 616 amino acids with a remarkable sequence homology to the putative precursor protein of trigramin from Trimeresurus grumineus venom (61% identity) and a large hemorrhagin, jararhagin, from the pit viper Bothrops jururucu venom (62% identity). Thus, ecarin, as well as jararhagin and trigramin, is translated as a precursor protein, which may be processed posttranslationally. The ecarin proprotein has a "cysteine switch" motif (-Pro-Lys- Met-Cys-Gly-Val-) similar to that involved in the activation of matrix metalloproteinase zymogens. The processed mature protein consists of 426 amino acid residues (residues 191 -616), showing the strongest sequence similarity with that of Russell's viper venom factor X activator (RVV-X) heavy chain (64% identity). Like RVV-X heavy chain, ecarin contains metalloproteinase, disintegrin, and cysteine-rich domains. The metalloproteinase domain has a typical zinc-chelating sequence (-His-Glu-Xaa-Xaa-His- Xaa-Xaa-Gly-Xga-Xaa-His-), as found in crayfish astacin. In the disintegrin domain of ecarin, the Arg- Gly-Asp sequence is replaced by Arg-Asp-Asp, as found in the disintegrin domains of RVV-X heavy chain (Arg-Asp-Glu) and a guinea pig sperm fusion protein, PH-30P (Thr-Asp-Glu). These findings show that while there are structural and evolutionary relationships among these proteins, each has a unique functional activity.