The Experts below are selected from a list of 144 Experts worldwide ranked by ideXlab platform
Yaohua Zhong - One of the best experts on this subject based on the ideXlab platform.
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proteomic analysis of the biomass hydrolytic potentials of penicillium oxalicum lignocellulolytic Enzyme System
Biotechnology for Biofuels, 2016Co-Authors: Wenxia Song, Guodong Liu, Yuanchao Qia, Guangsha Yao, Yaohua ZhongAbstract:Background The mining of high-performance Enzyme Systems is necessary to develop industrial lignocellulose bioconversion. Large amounts of cellulases and hemicellulases can be produced by Penicillium oxalicum. Hence, the Enzyme System of this hypercellulolytic fungus should be elucidated to help design optimum Enzyme Systems for effective biomass hydrolysis.
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Proteomic analysis of the biomass hydrolytic potentials of Penicillium oxalicum lignocellulolytic Enzyme System
Biotechnology for biofuels, 2016Co-Authors: Wenxia Song, Guodong Liu, Xiaolong Han, Yuanchao Qian, Guangshan Yao, Yaohua ZhongAbstract:The mining of high-performance Enzyme Systems is necessary to develop industrial lignocellulose bioconversion. Large amounts of cellulases and hemicellulases can be produced by Penicillium oxalicum. Hence, the Enzyme System of this hypercellulolytic fungus should be elucidated to help design optimum Enzyme Systems for effective biomass hydrolysis. The cellulolytic and xylanolytic activities of an SP Enzyme System prepared from P. oxalicum JU-A10 were comparatively analyzed. Results indicated that the fungus possesses a complete cellulolytic-xylanolytic Enzyme System. The cellobiohydrolase- and xylanase-specific activities of this System were higher than those of two other Enzyme Systems, i.e., ST from Trichoderma reesei SN1 and another commercial preparation Celluclast 1.5L. Delignified corncob residue (DCCR) could be hydrolyzed by SP to a greater extent than corncob residue (CCR). Beta-glucosidase (BG) supplemented in SP increased the ability of the System to hydrolyze DCCR and CCR, and resulted in a 64 % decrease in Enzyme dosage with the same glucose yield. The behaviors of the Enzyme components in the hydrolysis of CCR were further investigated by monitoring individual Enzyme dynamics. The total protein concentrations and cellobiohydrolase (CBH), endoglucanase (EG), and filter paper activities in the supernatants significantly decreased during saccharification. These findings were more evident in SP than in the other Enzyme Systems. The comparative proteomic analysis of the Enzyme Systems revealed that both SP and ST were rich in carbohydrate-degrading Enzymes and multiple non-hydrolytic proteins. A larger number of carbohydrate-binding modules 1 (CBM1) were also identified in SP than in ST. This difference might be linked to the greater adsorption to substrates and lower hydrolysis efficiency of SP Enzymes than ST during lignocellulose saccharification, because CBM1 not only targets Enzymes to insoluble cellulose but also leads to non-productive adsorption to lignin. Penicillium oxalicum can be applied to the biorefinery of lignocellulosic biomass. Its ability to degrade lignocellulosic substrates could be further improved by modifying its Enzyme System on the basis of Enzyme activity measurement and proteomic analysis. The proposed strategy may also be applied to other lignocellulolytic Enzyme Systems to enhance their hydrolytic performances rationally.
Dean R Appling - One of the best experts on this subject based on the ideXlab platform.
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Whole-cell detection by 13C NMR of metabolic flux through the C1-tetrahydrofolate synthase/serine hydroxymethyltransferase Enzyme System and effect of antifolate exposure in Saccharomyces cerevisiae.
Biochemistry, 1994Co-Authors: Laura B. Pasternack, David A. Laude, Dean R ApplingAbstract:Folate-mediated one-carbon metabolism is critical for the synthesis of numerous cellular constituents required for cell growth. A potential source of one-carbon units is formate. This one-carbon unit is activated to 10-formyltetrahydrofolate via the synthetase activity of the trifunctional Enzyme C1-tetrahydrofolate (THF) synthase for use in purine synthesis or can be further reduced to 5,10-methylene-THF by the dehydrogenase activity of the same Enzyme. 5,10-Methylene-THF is used by serine hydroxymethyltransferase (SHMT) in the synthesis of serine. Recently, 13C NMR has been used to establish that the C1-THF synthase/SHMT Enzyme System is the only route from formate to serine in vivo in the yeast Saccharomyces cerevisiae [Pasternack et al. (1992) Biochemistry 31, 8713-8719]. In vitro studies have considered the kinetics of the C1-THF synthase/SHMT Enzyme System in the catalytic conversion of formate to serine [Strong et al. (1987) J. Biol. Chem. 262, 12519-12525]. In the present work, we begin to study the kinetics of this two-Enzyme System in its natural environment. Provision of [13C]formate and direct detection of an intracellular accumulating pool of [3-13C]serine by 13C NMR of whole cells allow us to monitor the rate of flux through this Enzyme System in vivo. The rate of accumulation of soluble [3-13C]serine under [13C]formate-saturating conditions is 13.0 +/- 1.2 microM/min relative to an external standard of serine in D2O. The extracellular formate concentration at half-maximal flux was determined to be 900 microM.(ABSTRACT TRUNCATED AT 250 WORDS)
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whole cell detection by 13c nmr of metabolic flux through the c1 tetrahydrofolate synthase serine hydroxymethyltransferase Enzyme System and effect of antifolate exposure in saccharomyces cerevisiae
Biochemistry, 1994Co-Authors: Laura B. Pasternack, David A. Laude, Dean R ApplingAbstract:Folate-mediated one-carbon metabolism is critical for the synthesis of numerous cellular constituents required for cell growth. A potential source of one-carbon units is formate. This one-carbon unit is activated to 10-formyltetrahydrofolate via the synthetase activity of the trifunctional Enzyme C1-tetrahydrofolate (THF) synthase for use in purine synthesis or can be further reduced to 5,10-methylene-THF by the dehydrogenase activity of the same Enzyme. 5,10-Methylene-THF is used by serine hydroxymethyltransferase (SHMT) in the synthesis of serine. Recently, 13C NMR has been used to establish that the C1-THF synthase/SHMT Enzyme System is the only route from formate to serine in vivo in the yeast Saccharomyces cerevisiae [Pasternack et al. (1992) Biochemistry 31, 8713-8719]. In vitro studies have considered the kinetics of the C1-THF synthase/SHMT Enzyme System in the catalytic conversion of formate to serine [Strong et al. (1987) J. Biol. Chem. 262, 12519-12525]. In the present work, we begin to study the kinetics of this two-Enzyme System in its natural environment. Provision of [13C]formate and direct detection of an intracellular accumulating pool of [3-13C]serine by 13C NMR of whole cells allow us to monitor the rate of flux through this Enzyme System in vivo. The rate of accumulation of soluble [3-13C]serine under [13C]formate-saturating conditions is 13.0 +/- 1.2 microM/min relative to an external standard of serine in D2O. The extracellular formate concentration at half-maximal flux was determined to be 900 microM.(ABSTRACT TRUNCATED AT 250 WORDS)
Wenxia Song - One of the best experts on this subject based on the ideXlab platform.
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proteomic analysis of the biomass hydrolytic potentials of penicillium oxalicum lignocellulolytic Enzyme System
Biotechnology for Biofuels, 2016Co-Authors: Wenxia Song, Guodong Liu, Yuanchao Qia, Guangsha Yao, Yaohua ZhongAbstract:Background The mining of high-performance Enzyme Systems is necessary to develop industrial lignocellulose bioconversion. Large amounts of cellulases and hemicellulases can be produced by Penicillium oxalicum. Hence, the Enzyme System of this hypercellulolytic fungus should be elucidated to help design optimum Enzyme Systems for effective biomass hydrolysis.
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Proteomic analysis of the biomass hydrolytic potentials of Penicillium oxalicum lignocellulolytic Enzyme System
Biotechnology for biofuels, 2016Co-Authors: Wenxia Song, Guodong Liu, Xiaolong Han, Yuanchao Qian, Guangshan Yao, Yaohua ZhongAbstract:The mining of high-performance Enzyme Systems is necessary to develop industrial lignocellulose bioconversion. Large amounts of cellulases and hemicellulases can be produced by Penicillium oxalicum. Hence, the Enzyme System of this hypercellulolytic fungus should be elucidated to help design optimum Enzyme Systems for effective biomass hydrolysis. The cellulolytic and xylanolytic activities of an SP Enzyme System prepared from P. oxalicum JU-A10 were comparatively analyzed. Results indicated that the fungus possesses a complete cellulolytic-xylanolytic Enzyme System. The cellobiohydrolase- and xylanase-specific activities of this System were higher than those of two other Enzyme Systems, i.e., ST from Trichoderma reesei SN1 and another commercial preparation Celluclast 1.5L. Delignified corncob residue (DCCR) could be hydrolyzed by SP to a greater extent than corncob residue (CCR). Beta-glucosidase (BG) supplemented in SP increased the ability of the System to hydrolyze DCCR and CCR, and resulted in a 64 % decrease in Enzyme dosage with the same glucose yield. The behaviors of the Enzyme components in the hydrolysis of CCR were further investigated by monitoring individual Enzyme dynamics. The total protein concentrations and cellobiohydrolase (CBH), endoglucanase (EG), and filter paper activities in the supernatants significantly decreased during saccharification. These findings were more evident in SP than in the other Enzyme Systems. The comparative proteomic analysis of the Enzyme Systems revealed that both SP and ST were rich in carbohydrate-degrading Enzymes and multiple non-hydrolytic proteins. A larger number of carbohydrate-binding modules 1 (CBM1) were also identified in SP than in ST. This difference might be linked to the greater adsorption to substrates and lower hydrolysis efficiency of SP Enzymes than ST during lignocellulose saccharification, because CBM1 not only targets Enzymes to insoluble cellulose but also leads to non-productive adsorption to lignin. Penicillium oxalicum can be applied to the biorefinery of lignocellulosic biomass. Its ability to degrade lignocellulosic substrates could be further improved by modifying its Enzyme System on the basis of Enzyme activity measurement and proteomic analysis. The proposed strategy may also be applied to other lignocellulolytic Enzyme Systems to enhance their hydrolytic performances rationally.
Guodong Liu - One of the best experts on this subject based on the ideXlab platform.
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proteomic analysis of the biomass hydrolytic potentials of penicillium oxalicum lignocellulolytic Enzyme System
Biotechnology for Biofuels, 2016Co-Authors: Wenxia Song, Guodong Liu, Yuanchao Qia, Guangsha Yao, Yaohua ZhongAbstract:Background The mining of high-performance Enzyme Systems is necessary to develop industrial lignocellulose bioconversion. Large amounts of cellulases and hemicellulases can be produced by Penicillium oxalicum. Hence, the Enzyme System of this hypercellulolytic fungus should be elucidated to help design optimum Enzyme Systems for effective biomass hydrolysis.
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Proteomic analysis of the biomass hydrolytic potentials of Penicillium oxalicum lignocellulolytic Enzyme System
Biotechnology for biofuels, 2016Co-Authors: Wenxia Song, Guodong Liu, Xiaolong Han, Yuanchao Qian, Guangshan Yao, Yaohua ZhongAbstract:The mining of high-performance Enzyme Systems is necessary to develop industrial lignocellulose bioconversion. Large amounts of cellulases and hemicellulases can be produced by Penicillium oxalicum. Hence, the Enzyme System of this hypercellulolytic fungus should be elucidated to help design optimum Enzyme Systems for effective biomass hydrolysis. The cellulolytic and xylanolytic activities of an SP Enzyme System prepared from P. oxalicum JU-A10 were comparatively analyzed. Results indicated that the fungus possesses a complete cellulolytic-xylanolytic Enzyme System. The cellobiohydrolase- and xylanase-specific activities of this System were higher than those of two other Enzyme Systems, i.e., ST from Trichoderma reesei SN1 and another commercial preparation Celluclast 1.5L. Delignified corncob residue (DCCR) could be hydrolyzed by SP to a greater extent than corncob residue (CCR). Beta-glucosidase (BG) supplemented in SP increased the ability of the System to hydrolyze DCCR and CCR, and resulted in a 64 % decrease in Enzyme dosage with the same glucose yield. The behaviors of the Enzyme components in the hydrolysis of CCR were further investigated by monitoring individual Enzyme dynamics. The total protein concentrations and cellobiohydrolase (CBH), endoglucanase (EG), and filter paper activities in the supernatants significantly decreased during saccharification. These findings were more evident in SP than in the other Enzyme Systems. The comparative proteomic analysis of the Enzyme Systems revealed that both SP and ST were rich in carbohydrate-degrading Enzymes and multiple non-hydrolytic proteins. A larger number of carbohydrate-binding modules 1 (CBM1) were also identified in SP than in ST. This difference might be linked to the greater adsorption to substrates and lower hydrolysis efficiency of SP Enzymes than ST during lignocellulose saccharification, because CBM1 not only targets Enzymes to insoluble cellulose but also leads to non-productive adsorption to lignin. Penicillium oxalicum can be applied to the biorefinery of lignocellulosic biomass. Its ability to degrade lignocellulosic substrates could be further improved by modifying its Enzyme System on the basis of Enzyme activity measurement and proteomic analysis. The proposed strategy may also be applied to other lignocellulolytic Enzyme Systems to enhance their hydrolytic performances rationally.
Laura B. Pasternack - One of the best experts on this subject based on the ideXlab platform.
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Whole-cell detection by 13C NMR of metabolic flux through the C1-tetrahydrofolate synthase/serine hydroxymethyltransferase Enzyme System and effect of antifolate exposure in Saccharomyces cerevisiae.
Biochemistry, 1994Co-Authors: Laura B. Pasternack, David A. Laude, Dean R ApplingAbstract:Folate-mediated one-carbon metabolism is critical for the synthesis of numerous cellular constituents required for cell growth. A potential source of one-carbon units is formate. This one-carbon unit is activated to 10-formyltetrahydrofolate via the synthetase activity of the trifunctional Enzyme C1-tetrahydrofolate (THF) synthase for use in purine synthesis or can be further reduced to 5,10-methylene-THF by the dehydrogenase activity of the same Enzyme. 5,10-Methylene-THF is used by serine hydroxymethyltransferase (SHMT) in the synthesis of serine. Recently, 13C NMR has been used to establish that the C1-THF synthase/SHMT Enzyme System is the only route from formate to serine in vivo in the yeast Saccharomyces cerevisiae [Pasternack et al. (1992) Biochemistry 31, 8713-8719]. In vitro studies have considered the kinetics of the C1-THF synthase/SHMT Enzyme System in the catalytic conversion of formate to serine [Strong et al. (1987) J. Biol. Chem. 262, 12519-12525]. In the present work, we begin to study the kinetics of this two-Enzyme System in its natural environment. Provision of [13C]formate and direct detection of an intracellular accumulating pool of [3-13C]serine by 13C NMR of whole cells allow us to monitor the rate of flux through this Enzyme System in vivo. The rate of accumulation of soluble [3-13C]serine under [13C]formate-saturating conditions is 13.0 +/- 1.2 microM/min relative to an external standard of serine in D2O. The extracellular formate concentration at half-maximal flux was determined to be 900 microM.(ABSTRACT TRUNCATED AT 250 WORDS)
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whole cell detection by 13c nmr of metabolic flux through the c1 tetrahydrofolate synthase serine hydroxymethyltransferase Enzyme System and effect of antifolate exposure in saccharomyces cerevisiae
Biochemistry, 1994Co-Authors: Laura B. Pasternack, David A. Laude, Dean R ApplingAbstract:Folate-mediated one-carbon metabolism is critical for the synthesis of numerous cellular constituents required for cell growth. A potential source of one-carbon units is formate. This one-carbon unit is activated to 10-formyltetrahydrofolate via the synthetase activity of the trifunctional Enzyme C1-tetrahydrofolate (THF) synthase for use in purine synthesis or can be further reduced to 5,10-methylene-THF by the dehydrogenase activity of the same Enzyme. 5,10-Methylene-THF is used by serine hydroxymethyltransferase (SHMT) in the synthesis of serine. Recently, 13C NMR has been used to establish that the C1-THF synthase/SHMT Enzyme System is the only route from formate to serine in vivo in the yeast Saccharomyces cerevisiae [Pasternack et al. (1992) Biochemistry 31, 8713-8719]. In vitro studies have considered the kinetics of the C1-THF synthase/SHMT Enzyme System in the catalytic conversion of formate to serine [Strong et al. (1987) J. Biol. Chem. 262, 12519-12525]. In the present work, we begin to study the kinetics of this two-Enzyme System in its natural environment. Provision of [13C]formate and direct detection of an intracellular accumulating pool of [3-13C]serine by 13C NMR of whole cells allow us to monitor the rate of flux through this Enzyme System in vivo. The rate of accumulation of soluble [3-13C]serine under [13C]formate-saturating conditions is 13.0 +/- 1.2 microM/min relative to an external standard of serine in D2O. The extracellular formate concentration at half-maximal flux was determined to be 900 microM.(ABSTRACT TRUNCATED AT 250 WORDS)