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Pierre Abad - One of the best experts on this subject based on the ideXlab platform.

  • isolation of a cdna encoding a β 1 4 endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-par...

  • Isolation of a cDNA encoding a β-1,4-endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-Microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a β-1,4-endoglucanase devoid of a cellulose-binding domain

  • Isolation of a cDNA encoding a β-1,4-endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-Microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a β-1,4-endoglucanase devoid of a cellulose-binding domain

Marie-noëlle Rosso - One of the best experts on this subject based on the ideXlab platform.

  • isolation of a cdna encoding a β 1 4 endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-par...

  • Isolation of a cDNA encoding a β-1,4-endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-Microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a β-1,4-endoglucanase devoid of a cellulose-binding domain

  • Isolation of a cDNA encoding a β-1,4-endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-Microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a β-1,4-endoglucanase devoid of a cellulose-binding domain

Johanna Buchert - One of the best experts on this subject based on the ideXlab platform.

  • the effect of trichoderma reesei cellulases and hemicellulases on the paper technical properties of never dried bleached kraft pulp
    Cellulose, 1997
    Co-Authors: Tarja Oksanen, Johanna Buchert, Jaakko Pere, Liisa Viikari
    Abstract:

    Four purified cellulases, a xylanase and mannanase from Trichoderma reesei were used to treat never-dried bleached pine kraft pulp prior to refining, and the effects on pulp properties were evaluated. The enzymatic treatments hydrolysed up to 0.8% of pulp dry weight. The results demonstrated that the individual cellulases have profoundly different modes of action in modifying pulp carbohydrates. This is especially clear when comparing their effects at the same level of hydrolysis. Pretreatment with cellobiohydrolases I (CBH I) and II (CBH II) had virtually no effect on the development of pulp properties during refining, except for a slight decrease in strength properties. On the contrary, endoglucanase I (EG I) and endoglucanase II (EG II) improved the beatability of the pulp as measured by Schopper--Riegler value, sheet density and Gurley air resistance. Of the Endoglucanases, EG II was most effective in improving the beating response. The combinations of CBH I with EG I and EG II had similar effects on the pulp properties as the Endoglucanases alone, although the amount of hydrolysed cellulose was increased. Pretreatments with xylanase or mannanase did not appear to modify the pulp properties. The same enzyme treatments which improved the beatability, however, slightly impaired the pulp strength, especially tear index at the enzyme dosages used. When compared at a given level of cellulose hydrolysis, the negative effect of EG II on strength properties was more pronounced compared with EG I. Thus, the exploitation of cellulases for fibre treatments requires careful optimization of both enzyme composition and dosage. Since the Endoglucanases had no positive effect on the development of tensile strength, it is suggested that the explanation for the increased beating response is increased fibre breakage and formation of fines, rather than improved flexibilization.

  • modification of hardwood dissolving pulp with purifiedtrichoderma reesei cellulases
    Cellulose, 1996
    Co-Authors: Leena Rahkamo, Marianna Vehvilainen, Matti Dolk, Pertti Nousiainen, Matti Siikaaho, Liisa Viikari, Johanna Buchert
    Abstract:

    Hardwood dissolving pulp was treated with purifiedTrichoderma reeseiEndoglucanases and cellobiohydrolases. Endoglucanases were more efficient in hydrolysing pulp carbohydrates than were the cellobiohydrolases at the same protein dosage. Endoglucanases also lowered the viscosity and improved the alkaline solubility more dramatically. There was a clear correlation between the alkaline solubility and viscosity, and therefore the solubility could only be improved by lowering the viscosity of the pulp. At the same degree of cellulose degradation, endoglucanase II was found to be most effective in reducing the viscosity and thus improving the solubility. Cellobiohydrolases had a less pronounced effect on the viscosity or solubility.

  • modification of hardwood dissolving pulp with purifiedtrichoderma reesei cellulases
    Cellulose, 1996
    Co-Authors: Leena Rahkamo, Marianna Vehvilainen, Matti Dolk, Pertti Nousiainen, Matti Siikaaho, Liisa Viikari, Johanna Buchert
    Abstract:

    Hardwood dissolving pulp was treated with purifiedTrichoderma reeseiEndoglucanases and cellobiohydrolases. Endoglucanases were more efficient in hydrolysing pulp carbohydrates than were the cellobiohydrolases at the same protein dosage. Endoglucanases also lowered the viscosity and improved the alkaline solubility more dramatically. There was a clear correlation between the alkaline solubility and viscosity, and therefore the solubility could only be improved by lowering the viscosity of the pulp. At the same degree of cellulose degradation, endoglucanase II was found to be most effective in reducing the viscosity and thus improving the solubility. Cellobiohydrolases had a less pronounced effect on the viscosity or solubility.

Toshiaki Kono - One of the best experts on this subject based on the ideXlab platform.

  • purification and characterization of a new family 45 endoglucanase stce1 from staphylotrichum coccosporum and its overproduction in humicola insolens
    Applied and Environmental Microbiology, 2008
    Co-Authors: Jinichiro Koga, Atsushi Shimonaka, Yuko Baba, Tomoko Nishimura, Satoshi Hanamura, Toshiaki Kono
    Abstract:

    In the detergent industry, fungal Endoglucanases have been used to release microfibrils (defibrillation) from the surface of dyed cellulosic fabrics to enhance color brightness. Although Endoglucanases for laundry use must have various properties, such as a neutral or alkaline optimum pH, resistance to anionic surfactants and oxidizing agents (main components in detergents), and high defibrillation activity, all-purpose Endoglucanases have not been obtained yet. As a result of screening of Endoglucanases, a new family 45 endoglucanase (family 45 glycoside hydrolase), designated STCE1, was obtained and purified to apparent homogeneity from the culture supernatant of Staphylotrichum coccosporum NBRC 31817. The molecular mass of STCE1 was 49 kDa. The optimum pH for the carboxymethyl cellulase activity of STCE1 was 6.0, and the optimum temperature was 60°C. STCE1 was highly resistant to an anionic surfactant and an oxidizing agent. Furthermore, the defibrillation activities on dyed cotton and lyocell fabrics of STCE1 were higher than those of the other representative Endoglucanases tested. These results indicate that STCE1 is an all-purpose enzyme for laundry use. A gene encoding STCE1, designated the stce1 gene, was cloned from S. coccosporum, and the complete sequence was determined. STCE1 consisted of three distinct domains: an N-terminal catalytic domain (family 45), a linker domain, and a C-terminal carbohydrate-binding module (family 1). The amino acid sequences of the catalytic domain of STCE1 were phylogenetically close to those of the family 45 Endoglucanases EGL3, EGL4, and EGV from a Humicola sp. Hence, the stce1 gene was transferred into Humicola insolens and expressed. As a result, extremely high levels (0.90 mg protein per ml of culture supernatant, 27% of the total proteins) of the recombinant STCE1 were secreted as a mature form in the culture supernatant.

  • Amino acid regions of family 45 Endoglucanases involved in cotton defibrillation and in resistance to anionic surfactants and oxidizing agents.
    Bioscience biotechnology and biochemistry, 2006
    Co-Authors: Atsushi Shimonaka, Koichiro Murashima, Jinichiro Koga, Yuko Baba, Hidetoshi Kubota, Tomoko Nishimura, Toshiaki Kono
    Abstract:

    In the detergent industry, fungal Endoglucanases are used to release microfibrils from the surfaces of dyed cellulosic fabrics to enhance color brightness. Family 45 endoglucanase (glycoside hydrolase family 45, GH45) EGL3 from Humicola grisea is more resistant to anionic surfactants and oxidizing agents than family 45 endoglucanase RCE1 from Rhizopus oryzae, while in the present study, a catalytic domain of RCE1 had higher defibrillation activity on dyed cotton fabrics than did that of EGL3. To identify the amino acid regions involved in these properties, we compared the characteristics of RCE1, EGL3, and three chimeric Endoglucanases, in which each of the three regions of the catalytic domain of EGL3 was replaced by the corresponding region of the catalytic domain of RCE1. Amino acids in the N-terminal region were involved in resistance to anionic surfactants and oxidizing agents. Furthermore, amino acids in the region adjacent to the N-terminal region were involved in releasing microfibrils and in binding to dyed cotton fabrics, indicating that the binding of the amino acids in this region might be important in the release of microfibrils from dyed cotton fabrics.

  • Purification and Characterization of a New Endo-1,4-β- D -glucanase from Beltraniella portoricensis
    Bioscience biotechnology and biochemistry, 2005
    Co-Authors: Yuko Baba, Koichiro Murashima, Jinichiro Koga, Atsushi Shimonaka, Hidetoshi Kubota, Toshiaki Kono
    Abstract:

    A new endoglucanase, designated BCE1, produced by Beltraniella portoricensis, was purified from the culture supernatant. The N-terminal amino acid sequence suggests that BCE1 belongs to family 45 glycoside hydrolase (family 45 endoglucanase). The molecular mass of BCE1 was found to be 40 kDa by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH for the carboxymethyl cellulase (CMCase) activity of BCE1 was 4.5, and the optimum temperature was 55 degrees C. Among family 45 Endoglucanases, RCE1 and RCE2 from Rhizopus oryzae, PCE1 from Phycomyces nitens, and EGL3 and EGL4 from Humicola grisea, BCE1 was most resistant to anionic surfactant and oxidizing agent. These results indicate that BCE1 might prove to be a useful enzyme in the detergent industry.

  • Molecular Cloning of a Gene Encoding Endo-β-D-1,4-Glucanase PCE1 from Phycomyces nitens
    Bioscience biotechnology and biochemistry, 2004
    Co-Authors: Atsushi Shimonaka, Akitaka Nakane, Jinichiro Koga, Yuko Baba, Hidetoshi Kubota, Toshiaki Kono
    Abstract:

    We previously cloned three endoglucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae as the first cellulase genes from the subdivision Zygomycota. In this study, an endoglucanase gene, designated a pce1 gene, was cloned by plaque hybridization with the codon usage-optimized rce1 gene as a probe from Phycomyces nitens, a member of the subdivision Zygomycota. The pec1 gene had an open reading frame of 1,038 nucleotides encoding an endoglucanase (PCE1) of 346 amino acid residues. The amino acid sequence deduced from the pce1 gene consisted of a cellulose-binding domain (CBD) at the N terminus and of a catalytic domain belonging to family 45 glycoside hydrolase at the C terminus. PCE1 was purified to apparent homogeneity from the culture supernatant of P. nitens and the molecular mass was found to be 45 kDa. The optimum pH for the CMCase activity of PCE1 was 6.0, and the optimum temperature was 50 °C, the lowest among the family 45 Endoglucanases.

  • Purification and characterization of new endo-1,4-β-d-glucanases from Rhizopus oryzae
    Enzyme and Microbial Technology, 2002
    Co-Authors: Koichiro Murashima, Naomi Sumida, Jinichiro Koga, Tomoko Nishimura, Yuko Nakamura, Tastuki Moriya, Takashi Yaguchi, Toshiaki Kono
    Abstract:

    Abstract New extracellular Endoglucanases, designated RCE1 and RCE2, produced by Rhizopus oryzae isolated from the soil, were purified to apparent homogeneity from the culture supernatant. The molecular mass of RCE1 and that of RCE2 were found to be 41 kDa and 61 kDa, respectively. The N-terminal amino acid sequences of RCE1 and RCE2 showed high homology with those of the family I cellulose-binding domains. Internal amino acid sequences of RCE1 and RCE2 showed homology with that of the catalytic domain of EGV from Humicola insolens belonging to family 45 endoglucanase. The cellooligosaccharide hydrolysis patterns of RCE1 and RCE2 were similar to that of EGV from H. insolens. These results indicate that RCE1 and RCE2 are family 45 Endoglucanases having a cellulose binding domain at their N-terminus. RCE1 and RCE2 hydrolyzed carboxymethylcellulose (CMC), insoluble cellooligosaccharide (G33), cellohexaose, and cellopenpaose, but not Avicel, xylan, galactan, arabinan, mannan, or laminarin. The CMCase activity of both enzymes was inhibited by Cu 2+ , Zn 2+ , Co 2+ , and Pb 2+ . The optimum pH for the CMCase activity of both enzymes was found to be between pH value 5.0 and 6.0, and the optimum temperature was 55°C, the lowest among the family 45 Endoglucanases. These results indicate that RCE1 and RCE2 represent a new type of Endoglucanases having the lowest optimum temperature among the family 45 Endoglucanases.

Richard S Hussey - One of the best experts on this subject based on the ideXlab platform.

  • isolation of a cdna encoding a β 1 4 endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-par...

  • Isolation of a cDNA encoding a β-1,4-endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-Microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a β-1,4-endoglucanase devoid of a cellulose-binding domain

  • Isolation of a cDNA encoding a β-1,4-endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
    Molecular Plant-Microbe Interactions, 1999
    Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre Abad
    Abstract:

    A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a β-1,4-endoglucanase devoid of a cellulose-binding domain