The Experts below are selected from a list of 6219 Experts worldwide ranked by ideXlab platform
Krishanu Chakrabarti - One of the best experts on this subject based on the ideXlab platform.
-
Arg235 is an essential catalytic residue of Bacillus pumilus DKS1 Pectate lyase to degum ramie fibre
Biodegradation, 2010Co-Authors: Snehasish Basu, Arunava Roy, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Krishanu ChakrabartiAbstract:After 24 h of incubation with only purified Pectate lyase isolated from Bacillus pumilus DKS1 (EF467045), the weight loss of the ramie fibre was found to be 25%. To know the catalytic residue of Pectate lyase the pel gene encoding a Pectate lyase from the strain Bacillus pumilus DKS1 was cloned in E. coli XL1Blue and expressed in E. coli BL21 (DE3) pLysS. The pel gene was sequenced and showed 1032 bp length. After purification using CM-Sepharose the enzyme showed molecular weight of 35 kDa and maximal enzymatic activity was observed at 60°C and a pH range of 8.5–9.0. Both Ca2+ and Mn2+ ions were required for activity on Na-Pectate salt substrates, while the enzyme was strongly inhibited by Zn2+ and EDTA. The deduced nucleotide sequence of the DKS1 Pectate lyase (EU652988) showed 90% homology to Pectate lyases from Bacillus pumilus SAFR-032 (CP000813). The 3D structure as well as the catalytic residues was predicted using EasyPred software and Catalytic Site Atlas (CSA), respectively. Site directed mutagenesis confirmed that arginine is an essential catalytic residue of DKS1 Pectate lyase.
-
thermodynamic characterization of a highly thermoactive extracellular Pectate lyase from a new isolate bacillus pumilus dks1
Bioresource Technology, 2008Co-Authors: Snehasish Basu, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Manabendra N Saha, Krishanu ChakrabartiAbstract:Abstract An extracellular Pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium. Using ion-exchange and gel filtration chromatography, this enzyme was purified and found to have a molecular weight of around 35 kDa. The purified enzyme exhibited maximal activity at a temperature of 75 °C and pH 8.5. The presence of 1 mM calcium and manganese enhanced Pectate lyase activity and was strongly inhibited by zinc, nickel and EDTA. The thermal inactivation studies revealed an entropy–enthalpy compensation pattern below a critical temperature. The alkaliphilicity and high thermostability of this Pectate lyase may have potential implications in fibre degumming.
Snehasish Basu - One of the best experts on this subject based on the ideXlab platform.
-
Arg235 is an essential catalytic residue of Bacillus pumilus DKS1 Pectate lyase to degum ramie fibre
Biodegradation, 2010Co-Authors: Snehasish Basu, Arunava Roy, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Krishanu ChakrabartiAbstract:After 24 h of incubation with only purified Pectate lyase isolated from Bacillus pumilus DKS1 (EF467045), the weight loss of the ramie fibre was found to be 25%. To know the catalytic residue of Pectate lyase the pel gene encoding a Pectate lyase from the strain Bacillus pumilus DKS1 was cloned in E. coli XL1Blue and expressed in E. coli BL21 (DE3) pLysS. The pel gene was sequenced and showed 1032 bp length. After purification using CM-Sepharose the enzyme showed molecular weight of 35 kDa and maximal enzymatic activity was observed at 60°C and a pH range of 8.5–9.0. Both Ca2+ and Mn2+ ions were required for activity on Na-Pectate salt substrates, while the enzyme was strongly inhibited by Zn2+ and EDTA. The deduced nucleotide sequence of the DKS1 Pectate lyase (EU652988) showed 90% homology to Pectate lyases from Bacillus pumilus SAFR-032 (CP000813). The 3D structure as well as the catalytic residues was predicted using EasyPred software and Catalytic Site Atlas (CSA), respectively. Site directed mutagenesis confirmed that arginine is an essential catalytic residue of DKS1 Pectate lyase.
-
thermodynamic characterization of a highly thermoactive extracellular Pectate lyase from a new isolate bacillus pumilus dks1
Bioresource Technology, 2008Co-Authors: Snehasish Basu, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Manabendra N Saha, Krishanu ChakrabartiAbstract:Abstract An extracellular Pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium. Using ion-exchange and gel filtration chromatography, this enzyme was purified and found to have a molecular weight of around 35 kDa. The purified enzyme exhibited maximal activity at a temperature of 75 °C and pH 8.5. The presence of 1 mM calcium and manganese enhanced Pectate lyase activity and was strongly inhibited by zinc, nickel and EDTA. The thermal inactivation studies revealed an entropy–enthalpy compensation pattern below a critical temperature. The alkaliphilicity and high thermostability of this Pectate lyase may have potential implications in fibre degumming.
Dhrubajyoti Chattopadhyay - One of the best experts on this subject based on the ideXlab platform.
-
Arg235 is an essential catalytic residue of Bacillus pumilus DKS1 Pectate lyase to degum ramie fibre
Biodegradation, 2010Co-Authors: Snehasish Basu, Arunava Roy, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Krishanu ChakrabartiAbstract:After 24 h of incubation with only purified Pectate lyase isolated from Bacillus pumilus DKS1 (EF467045), the weight loss of the ramie fibre was found to be 25%. To know the catalytic residue of Pectate lyase the pel gene encoding a Pectate lyase from the strain Bacillus pumilus DKS1 was cloned in E. coli XL1Blue and expressed in E. coli BL21 (DE3) pLysS. The pel gene was sequenced and showed 1032 bp length. After purification using CM-Sepharose the enzyme showed molecular weight of 35 kDa and maximal enzymatic activity was observed at 60°C and a pH range of 8.5–9.0. Both Ca2+ and Mn2+ ions were required for activity on Na-Pectate salt substrates, while the enzyme was strongly inhibited by Zn2+ and EDTA. The deduced nucleotide sequence of the DKS1 Pectate lyase (EU652988) showed 90% homology to Pectate lyases from Bacillus pumilus SAFR-032 (CP000813). The 3D structure as well as the catalytic residues was predicted using EasyPred software and Catalytic Site Atlas (CSA), respectively. Site directed mutagenesis confirmed that arginine is an essential catalytic residue of DKS1 Pectate lyase.
-
thermodynamic characterization of a highly thermoactive extracellular Pectate lyase from a new isolate bacillus pumilus dks1
Bioresource Technology, 2008Co-Authors: Snehasish Basu, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Manabendra N Saha, Krishanu ChakrabartiAbstract:Abstract An extracellular Pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium. Using ion-exchange and gel filtration chromatography, this enzyme was purified and found to have a molecular weight of around 35 kDa. The purified enzyme exhibited maximal activity at a temperature of 75 °C and pH 8.5. The presence of 1 mM calcium and manganese enhanced Pectate lyase activity and was strongly inhibited by zinc, nickel and EDTA. The thermal inactivation studies revealed an entropy–enthalpy compensation pattern below a critical temperature. The alkaliphilicity and high thermostability of this Pectate lyase may have potential implications in fibre degumming.
Amit Bera - One of the best experts on this subject based on the ideXlab platform.
-
Arg235 is an essential catalytic residue of Bacillus pumilus DKS1 Pectate lyase to degum ramie fibre
Biodegradation, 2010Co-Authors: Snehasish Basu, Arunava Roy, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Krishanu ChakrabartiAbstract:After 24 h of incubation with only purified Pectate lyase isolated from Bacillus pumilus DKS1 (EF467045), the weight loss of the ramie fibre was found to be 25%. To know the catalytic residue of Pectate lyase the pel gene encoding a Pectate lyase from the strain Bacillus pumilus DKS1 was cloned in E. coli XL1Blue and expressed in E. coli BL21 (DE3) pLysS. The pel gene was sequenced and showed 1032 bp length. After purification using CM-Sepharose the enzyme showed molecular weight of 35 kDa and maximal enzymatic activity was observed at 60°C and a pH range of 8.5–9.0. Both Ca2+ and Mn2+ ions were required for activity on Na-Pectate salt substrates, while the enzyme was strongly inhibited by Zn2+ and EDTA. The deduced nucleotide sequence of the DKS1 Pectate lyase (EU652988) showed 90% homology to Pectate lyases from Bacillus pumilus SAFR-032 (CP000813). The 3D structure as well as the catalytic residues was predicted using EasyPred software and Catalytic Site Atlas (CSA), respectively. Site directed mutagenesis confirmed that arginine is an essential catalytic residue of DKS1 Pectate lyase.
-
thermodynamic characterization of a highly thermoactive extracellular Pectate lyase from a new isolate bacillus pumilus dks1
Bioresource Technology, 2008Co-Authors: Snehasish Basu, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Manabendra N Saha, Krishanu ChakrabartiAbstract:Abstract An extracellular Pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium. Using ion-exchange and gel filtration chromatography, this enzyme was purified and found to have a molecular weight of around 35 kDa. The purified enzyme exhibited maximal activity at a temperature of 75 °C and pH 8.5. The presence of 1 mM calcium and manganese enhanced Pectate lyase activity and was strongly inhibited by zinc, nickel and EDTA. The thermal inactivation studies revealed an entropy–enthalpy compensation pattern below a critical temperature. The alkaliphilicity and high thermostability of this Pectate lyase may have potential implications in fibre degumming.
Abhrajyoti Ghosh - One of the best experts on this subject based on the ideXlab platform.
-
Arg235 is an essential catalytic residue of Bacillus pumilus DKS1 Pectate lyase to degum ramie fibre
Biodegradation, 2010Co-Authors: Snehasish Basu, Arunava Roy, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Krishanu ChakrabartiAbstract:After 24 h of incubation with only purified Pectate lyase isolated from Bacillus pumilus DKS1 (EF467045), the weight loss of the ramie fibre was found to be 25%. To know the catalytic residue of Pectate lyase the pel gene encoding a Pectate lyase from the strain Bacillus pumilus DKS1 was cloned in E. coli XL1Blue and expressed in E. coli BL21 (DE3) pLysS. The pel gene was sequenced and showed 1032 bp length. After purification using CM-Sepharose the enzyme showed molecular weight of 35 kDa and maximal enzymatic activity was observed at 60°C and a pH range of 8.5–9.0. Both Ca2+ and Mn2+ ions were required for activity on Na-Pectate salt substrates, while the enzyme was strongly inhibited by Zn2+ and EDTA. The deduced nucleotide sequence of the DKS1 Pectate lyase (EU652988) showed 90% homology to Pectate lyases from Bacillus pumilus SAFR-032 (CP000813). The 3D structure as well as the catalytic residues was predicted using EasyPred software and Catalytic Site Atlas (CSA), respectively. Site directed mutagenesis confirmed that arginine is an essential catalytic residue of DKS1 Pectate lyase.
-
thermodynamic characterization of a highly thermoactive extracellular Pectate lyase from a new isolate bacillus pumilus dks1
Bioresource Technology, 2008Co-Authors: Snehasish Basu, Abhrajyoti Ghosh, Amit Bera, Dhrubajyoti Chattopadhyay, Manabendra N Saha, Krishanu ChakrabartiAbstract:Abstract An extracellular Pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium. Using ion-exchange and gel filtration chromatography, this enzyme was purified and found to have a molecular weight of around 35 kDa. The purified enzyme exhibited maximal activity at a temperature of 75 °C and pH 8.5. The presence of 1 mM calcium and manganese enhanced Pectate lyase activity and was strongly inhibited by zinc, nickel and EDTA. The thermal inactivation studies revealed an entropy–enthalpy compensation pattern below a critical temperature. The alkaliphilicity and high thermostability of this Pectate lyase may have potential implications in fibre degumming.