The Experts below are selected from a list of 174132 Experts worldwide ranked by ideXlab platform
Jayanta Kumar Basu - One of the best experts on this subject based on the ideXlab platform.
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effects of process variables and additives on mustard oil hydrolysis by porcine pancreas lipase
Brazilian Journal of Chemical Engineering, 2012Co-Authors: Debajyoti Goswami, Jayanta Kumar BasuAbstract:Selective hydrolysis of brown mustard oil (from Brassica juncea) with regioselective porcine pancreas lipase was studied in this work. Buffer and oil phase were considered as the continuous and dispersed phases, respectively. Effects of speed of agitation, pH of the buffer phase, temperature, buffer-oil ratio and Enzyme Concentration on hydrolysis were observed. The best combination of process variables was: 900 rpm, pH 9, 35 oC, buffer-oil ratio of 1:1 and Enzyme Concentration of 10 mg/g oil. These standard conditions led to 50% hydrolysis and selective production of 55% erucic acid in 6 h. Cations like Mg2+ and Ca2+ increased hydrolysis, but Cu2+ strongly inhibited it. Organic solvents decreased hydrolysis, though the decrease was minimum for isooctane. A mixed surfactant comprising of Span 80 and Tween 80 increased erucic acid production by 57% at a buffer-oil ratio of 0.2:1.
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maximization of bioconversion of castor oil into ricinoleic acid by response surface methodology
Bioresource Technology, 2009Co-Authors: Debajyoti Goswami, Ramkrishna Sen, Jayanta Kumar BasuAbstract:Abstract In this study, response surface methodology was applied to optimize process variables like temperature, pH, Enzyme Concentration (mg/g oil), and buffer Concentration (g/g oil) for hydrolysis of castor oil using Candida rugosa lipase. A 2 4 full factorial central composite design was used to develop the quadratic model that was subsequently optimized and the optimal conditions were as follows: temperature 40 °C, pH 7.72, Enzyme Concentration 5.28 mg/g oil, buffer Concentration 1 g/g oil and there was 65.5% conversion in 6 h. These predicted optimal conditions agreed well with the experimental results. This is the first report on the application of response surface methodology in castor oil hydrolysis using C. rugosa lipase with higher percentage conversion in 6 h.
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Surfactant enhanced ricinoleic acid production using Candida rugosa lipase
Bioresource technology, 2009Co-Authors: Debajyoti Goswami, Ramkrishna Sen, Jayanta Kumar BasuAbstract:Abstract In this study, ricinoleic acid was produced on surfactant enhanced castor oil hydrolysis using Candida rugosa lipase. The most effective surfactant was Span 80. Employing fractional factorial design, the most suitable temperature and surfactant Concentration were found to be 31 °C and 0.257% (w/w in buffer) respectively whereas pH, Enzyme Concentration, buffer Concentration and agitation were identified as the most significant independent variables. A 2 4 full factorial central composite design was applied and the optimal conditions were found to be pH 7.0, Enzyme Concentration 7.42 mg/g oil, buffer Concentration 0.20 g/g oil and agitation 1400 rpm with the maximum response of 76% in 4 h. The most important variable was pH, whereas Enzyme and buffer Concentrations also showed pronounced effect on response. This is the first report on the application of response surface methodology for optimizing surfactant enhanced ricinoleic acid production using C. rugosa lipase.
Anu Koivula - One of the best experts on this subject based on the ideXlab platform.
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single molecule imaging analysis of elementary reaction steps of trichoderma reesei cellobiohydrolase i cel7a hydrolyzing crystalline cellulose iα and iiii
Journal of Biological Chemistry, 2014Co-Authors: Yusuke Shibafuji, Akihiko Nakamura, Takayuki Uchihashi, Naohisa Sugimoto, Shingo Fukuda, Hiroki Watanabe, Masahiro Samejima, Toshio Ando, Hiroyuki Noji, Anu KoivulaAbstract:Abstract Trichoderma reesei cellobiohydrolase I (TrCel7A) is a molecular motor that directly hydrolyzes crystalline celluloses into water-soluble cellobioses. It has recently drawn attention as a tool that could be used to convert cellulosic materials into biofuel. However, detailed mechanisms of action, including elementary reaction steps such as binding, processive hydrolysis, and dissociation, have not been thoroughly explored owing to the inherent challenges associated with monitoring reactions occurring at the solid/liquid interface. The crystalline cellulose Iα and IIII were previously reported as substrates with different crystalline forms and different susceptibilities to hydrolysis by TrCel7A. In this study, we observed that different susceptibilities of cellulose Iα and IIII are highly dependent on Enzyme Concentration, and at nanomolar Enzyme Concentration, TrCel7A shows similar rates of hydrolysis against cellulose Iα and IIII. Using single-molecule fluorescence microscopy and high-speed atomic force microscopy, we also determined kinetic constants of the elementary reaction steps for TrCel7A against cellulose Iα and IIII. These measurements were performed at picomolar Enzyme Concentration in which density of TrCel7A on crystalline cellulose was very low. Under this condition, TrCel7A displayed similar binding and dissociation rate constants for cellulose Iα and IIII, and similar fractions of productive binding on cellulose Iα and IIII. Furthermore, once productively bound, TrCel7A processively hydrolyzes and moves along cellulose Iα and IIII with similar translational rates. With structural models of cellulose Iα and IIII, we propose that different susceptibilities at high TrCel7A Concentration arise from surface properties of substrate, including ratio of hydrophobic surface and number of available lanes.
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single molecule imaging analysis of elementary reaction steps of trichoderma reesei cellobiohydrolase i cel7a hydrolyzing crystalline cellulose iα and iiii
Journal of Biological Chemistry, 2014Co-Authors: Yusuke Shibafuji, Akihiko Nakamura, Takayuki Uchihashi, Naohisa Sugimoto, Shingo Fukuda, Hiroki Watanabe, Masahiro Samejima, Toshio Ando, Hiroyuki Noji, Anu KoivulaAbstract:Trichoderma reesei cellobiohydrolase I (TrCel7A) is a molecular motor that directly hydrolyzes crystalline celluloses into water-soluble cellobioses. It has recently drawn attention as a tool that could be used to convert cellulosic materials into biofuel. However, detailed mechanisms of action, including elementary reaction steps such as binding, processive hydrolysis, and dissociation, have not been thoroughly explored because of the inherent challenges associated with monitoring reactions occurring at the solid/liquid interface. The crystalline cellulose Iα and IIII were previously reported as substrates with different crystalline forms and different susceptibilities to hydrolysis by TrCel7A. In this study, we observed that different susceptibilities of cellulose Iα and IIII are highly dependent on Enzyme Concentration, and at nanomolar Enzyme Concentration, TrCel7A shows similar rates of hydrolysis against cellulose Iα and IIII. Using single-molecule fluorescence microscopy and high speed atomic force microscopy, we also determined kinetic constants of the elementary reaction steps for TrCel7A against cellulose Iα and IIII. These measurements were performed at picomolar Enzyme Concentration in which density of TrCel7A on crystalline cellulose was very low. Under this condition, TrCel7A displayed similar binding and dissociation rate constants for cellulose Iα and IIII and similar fractions of productive binding on cellulose Iα and IIII. Furthermore, once productively bound, TrCel7A processively hydrolyzes and moves along cellulose Iα and IIII with similar translational rates. With structural models of cellulose Iα and IIII, we propose that different susceptibilities at high TrCel7A Concentration arise from surface properties of substrate, including ratio of hydrophobic surface and number of available lanes.
Debajyoti Goswami - One of the best experts on this subject based on the ideXlab platform.
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effects of process variables and additives on mustard oil hydrolysis by porcine pancreas lipase
Brazilian Journal of Chemical Engineering, 2012Co-Authors: Debajyoti Goswami, Jayanta Kumar BasuAbstract:Selective hydrolysis of brown mustard oil (from Brassica juncea) with regioselective porcine pancreas lipase was studied in this work. Buffer and oil phase were considered as the continuous and dispersed phases, respectively. Effects of speed of agitation, pH of the buffer phase, temperature, buffer-oil ratio and Enzyme Concentration on hydrolysis were observed. The best combination of process variables was: 900 rpm, pH 9, 35 oC, buffer-oil ratio of 1:1 and Enzyme Concentration of 10 mg/g oil. These standard conditions led to 50% hydrolysis and selective production of 55% erucic acid in 6 h. Cations like Mg2+ and Ca2+ increased hydrolysis, but Cu2+ strongly inhibited it. Organic solvents decreased hydrolysis, though the decrease was minimum for isooctane. A mixed surfactant comprising of Span 80 and Tween 80 increased erucic acid production by 57% at a buffer-oil ratio of 0.2:1.
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maximization of bioconversion of castor oil into ricinoleic acid by response surface methodology
Bioresource Technology, 2009Co-Authors: Debajyoti Goswami, Ramkrishna Sen, Jayanta Kumar BasuAbstract:Abstract In this study, response surface methodology was applied to optimize process variables like temperature, pH, Enzyme Concentration (mg/g oil), and buffer Concentration (g/g oil) for hydrolysis of castor oil using Candida rugosa lipase. A 2 4 full factorial central composite design was used to develop the quadratic model that was subsequently optimized and the optimal conditions were as follows: temperature 40 °C, pH 7.72, Enzyme Concentration 5.28 mg/g oil, buffer Concentration 1 g/g oil and there was 65.5% conversion in 6 h. These predicted optimal conditions agreed well with the experimental results. This is the first report on the application of response surface methodology in castor oil hydrolysis using C. rugosa lipase with higher percentage conversion in 6 h.
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Surfactant enhanced ricinoleic acid production using Candida rugosa lipase
Bioresource technology, 2009Co-Authors: Debajyoti Goswami, Ramkrishna Sen, Jayanta Kumar BasuAbstract:Abstract In this study, ricinoleic acid was produced on surfactant enhanced castor oil hydrolysis using Candida rugosa lipase. The most effective surfactant was Span 80. Employing fractional factorial design, the most suitable temperature and surfactant Concentration were found to be 31 °C and 0.257% (w/w in buffer) respectively whereas pH, Enzyme Concentration, buffer Concentration and agitation were identified as the most significant independent variables. A 2 4 full factorial central composite design was applied and the optimal conditions were found to be pH 7.0, Enzyme Concentration 7.42 mg/g oil, buffer Concentration 0.20 g/g oil and agitation 1400 rpm with the maximum response of 76% in 4 h. The most important variable was pH, whereas Enzyme and buffer Concentrations also showed pronounced effect on response. This is the first report on the application of response surface methodology for optimizing surfactant enhanced ricinoleic acid production using C. rugosa lipase.
Yusuke Shibafuji - One of the best experts on this subject based on the ideXlab platform.
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single molecule imaging analysis of elementary reaction steps of trichoderma reesei cellobiohydrolase i cel7a hydrolyzing crystalline cellulose iα and iiii
Journal of Biological Chemistry, 2014Co-Authors: Yusuke Shibafuji, Akihiko Nakamura, Takayuki Uchihashi, Naohisa Sugimoto, Shingo Fukuda, Hiroki Watanabe, Masahiro Samejima, Toshio Ando, Hiroyuki Noji, Anu KoivulaAbstract:Abstract Trichoderma reesei cellobiohydrolase I (TrCel7A) is a molecular motor that directly hydrolyzes crystalline celluloses into water-soluble cellobioses. It has recently drawn attention as a tool that could be used to convert cellulosic materials into biofuel. However, detailed mechanisms of action, including elementary reaction steps such as binding, processive hydrolysis, and dissociation, have not been thoroughly explored owing to the inherent challenges associated with monitoring reactions occurring at the solid/liquid interface. The crystalline cellulose Iα and IIII were previously reported as substrates with different crystalline forms and different susceptibilities to hydrolysis by TrCel7A. In this study, we observed that different susceptibilities of cellulose Iα and IIII are highly dependent on Enzyme Concentration, and at nanomolar Enzyme Concentration, TrCel7A shows similar rates of hydrolysis against cellulose Iα and IIII. Using single-molecule fluorescence microscopy and high-speed atomic force microscopy, we also determined kinetic constants of the elementary reaction steps for TrCel7A against cellulose Iα and IIII. These measurements were performed at picomolar Enzyme Concentration in which density of TrCel7A on crystalline cellulose was very low. Under this condition, TrCel7A displayed similar binding and dissociation rate constants for cellulose Iα and IIII, and similar fractions of productive binding on cellulose Iα and IIII. Furthermore, once productively bound, TrCel7A processively hydrolyzes and moves along cellulose Iα and IIII with similar translational rates. With structural models of cellulose Iα and IIII, we propose that different susceptibilities at high TrCel7A Concentration arise from surface properties of substrate, including ratio of hydrophobic surface and number of available lanes.
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single molecule imaging analysis of elementary reaction steps of trichoderma reesei cellobiohydrolase i cel7a hydrolyzing crystalline cellulose iα and iiii
Journal of Biological Chemistry, 2014Co-Authors: Yusuke Shibafuji, Akihiko Nakamura, Takayuki Uchihashi, Naohisa Sugimoto, Shingo Fukuda, Hiroki Watanabe, Masahiro Samejima, Toshio Ando, Hiroyuki Noji, Anu KoivulaAbstract:Trichoderma reesei cellobiohydrolase I (TrCel7A) is a molecular motor that directly hydrolyzes crystalline celluloses into water-soluble cellobioses. It has recently drawn attention as a tool that could be used to convert cellulosic materials into biofuel. However, detailed mechanisms of action, including elementary reaction steps such as binding, processive hydrolysis, and dissociation, have not been thoroughly explored because of the inherent challenges associated with monitoring reactions occurring at the solid/liquid interface. The crystalline cellulose Iα and IIII were previously reported as substrates with different crystalline forms and different susceptibilities to hydrolysis by TrCel7A. In this study, we observed that different susceptibilities of cellulose Iα and IIII are highly dependent on Enzyme Concentration, and at nanomolar Enzyme Concentration, TrCel7A shows similar rates of hydrolysis against cellulose Iα and IIII. Using single-molecule fluorescence microscopy and high speed atomic force microscopy, we also determined kinetic constants of the elementary reaction steps for TrCel7A against cellulose Iα and IIII. These measurements were performed at picomolar Enzyme Concentration in which density of TrCel7A on crystalline cellulose was very low. Under this condition, TrCel7A displayed similar binding and dissociation rate constants for cellulose Iα and IIII and similar fractions of productive binding on cellulose Iα and IIII. Furthermore, once productively bound, TrCel7A processively hydrolyzes and moves along cellulose Iα and IIII with similar translational rates. With structural models of cellulose Iα and IIII, we propose that different susceptibilities at high TrCel7A Concentration arise from surface properties of substrate, including ratio of hydrophobic surface and number of available lanes.
Toshio Ando - One of the best experts on this subject based on the ideXlab platform.
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single molecule imaging analysis of elementary reaction steps of trichoderma reesei cellobiohydrolase i cel7a hydrolyzing crystalline cellulose iα and iiii
Journal of Biological Chemistry, 2014Co-Authors: Yusuke Shibafuji, Akihiko Nakamura, Takayuki Uchihashi, Naohisa Sugimoto, Shingo Fukuda, Hiroki Watanabe, Masahiro Samejima, Toshio Ando, Hiroyuki Noji, Anu KoivulaAbstract:Abstract Trichoderma reesei cellobiohydrolase I (TrCel7A) is a molecular motor that directly hydrolyzes crystalline celluloses into water-soluble cellobioses. It has recently drawn attention as a tool that could be used to convert cellulosic materials into biofuel. However, detailed mechanisms of action, including elementary reaction steps such as binding, processive hydrolysis, and dissociation, have not been thoroughly explored owing to the inherent challenges associated with monitoring reactions occurring at the solid/liquid interface. The crystalline cellulose Iα and IIII were previously reported as substrates with different crystalline forms and different susceptibilities to hydrolysis by TrCel7A. In this study, we observed that different susceptibilities of cellulose Iα and IIII are highly dependent on Enzyme Concentration, and at nanomolar Enzyme Concentration, TrCel7A shows similar rates of hydrolysis against cellulose Iα and IIII. Using single-molecule fluorescence microscopy and high-speed atomic force microscopy, we also determined kinetic constants of the elementary reaction steps for TrCel7A against cellulose Iα and IIII. These measurements were performed at picomolar Enzyme Concentration in which density of TrCel7A on crystalline cellulose was very low. Under this condition, TrCel7A displayed similar binding and dissociation rate constants for cellulose Iα and IIII, and similar fractions of productive binding on cellulose Iα and IIII. Furthermore, once productively bound, TrCel7A processively hydrolyzes and moves along cellulose Iα and IIII with similar translational rates. With structural models of cellulose Iα and IIII, we propose that different susceptibilities at high TrCel7A Concentration arise from surface properties of substrate, including ratio of hydrophobic surface and number of available lanes.
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single molecule imaging analysis of elementary reaction steps of trichoderma reesei cellobiohydrolase i cel7a hydrolyzing crystalline cellulose iα and iiii
Journal of Biological Chemistry, 2014Co-Authors: Yusuke Shibafuji, Akihiko Nakamura, Takayuki Uchihashi, Naohisa Sugimoto, Shingo Fukuda, Hiroki Watanabe, Masahiro Samejima, Toshio Ando, Hiroyuki Noji, Anu KoivulaAbstract:Trichoderma reesei cellobiohydrolase I (TrCel7A) is a molecular motor that directly hydrolyzes crystalline celluloses into water-soluble cellobioses. It has recently drawn attention as a tool that could be used to convert cellulosic materials into biofuel. However, detailed mechanisms of action, including elementary reaction steps such as binding, processive hydrolysis, and dissociation, have not been thoroughly explored because of the inherent challenges associated with monitoring reactions occurring at the solid/liquid interface. The crystalline cellulose Iα and IIII were previously reported as substrates with different crystalline forms and different susceptibilities to hydrolysis by TrCel7A. In this study, we observed that different susceptibilities of cellulose Iα and IIII are highly dependent on Enzyme Concentration, and at nanomolar Enzyme Concentration, TrCel7A shows similar rates of hydrolysis against cellulose Iα and IIII. Using single-molecule fluorescence microscopy and high speed atomic force microscopy, we also determined kinetic constants of the elementary reaction steps for TrCel7A against cellulose Iα and IIII. These measurements were performed at picomolar Enzyme Concentration in which density of TrCel7A on crystalline cellulose was very low. Under this condition, TrCel7A displayed similar binding and dissociation rate constants for cellulose Iα and IIII and similar fractions of productive binding on cellulose Iα and IIII. Furthermore, once productively bound, TrCel7A processively hydrolyzes and moves along cellulose Iα and IIII with similar translational rates. With structural models of cellulose Iα and IIII, we propose that different susceptibilities at high TrCel7A Concentration arise from surface properties of substrate, including ratio of hydrophobic surface and number of available lanes.