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M. Chandrasekaran - One of the best experts on this subject based on the ideXlab platform.
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Characterization of an extracellular alkaline serine protease from marine Engyodontium Album BTMFS10
Journal of Industrial Microbiology & Biotechnology, 2011Co-Authors: Sreeja Chellappan, Sarita,g Bhat, C. Jasmin, K. K. Elyas, Soorej M. Basheer, Archana Kishore, M. ChandrasekaranAbstract:An alkaline protease from marine Engyodontium Album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme. K _m, V _max, and K _cat of the enzyme were 4.727 × 10^−2 mg/ml, 394.68 U, and 4.2175 × 10^−2 s^−1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65°C), with maximum activity at pH 11 and 60°C. CaCl_2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65°C. Hg^2+, Cu^2+, Fe^3+, Zn^2+, Cd^+, and Al^3+ inhibited enzyme activity, while 1 mM Co^2+ enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications.
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Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium Album BTMFS10
World Journal of Microbiology and Biotechnology, 2010Co-Authors: C. Jasmin, Sreeja Chellappan, Sarita,g Bhat, Rajeev K. Sukumaran, K. K. Elyas, M. ChandrasekaranAbstract:An alkaline protease gene ( Eap ) was isolated for the first time from a marine fungus, Engyodontium Album . Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium Album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca^2+ binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein.
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production purification and partial characterization of a novel protease from marine Engyodontium Album btmfs10 under solid state fermentation
Process Biochemistry, 2006Co-Authors: Sreeja Chellappan, Sarita,g Bhat, C. Jasmin, K. K. Elyas, Soorej M. Basheer, M. ChandrasekaranAbstract:Engyodontium Album isolated from marine sediment produced protease, which was active at pH 11. Process parameters influencing the production of alkaline protease by marine E. Album was optimized. Particle size of <425 μm, 60% initial moisture content and incubation at 25 °C for 120 h were optimal for protease production under solid state fermentation (SSF) using wheat bran. The organism has two optimal pH (5 and 10) for maximal enzyme production. Sucrose as carbon source, ammonium hydrogen carbonate as additional inorganic nitrogen source and amino acid leucine enhanced enzyme production during SSF. The protease was purified and partially characterized. A 16-fold purified enzyme was obtained after ammonium sulphate precipitation and ion-exchange chromatography. Molecular weight of the purified enzyme protein was recorded approximately 38 kDa by SDS-PAGE. The enzyme showed maximum activity at pH 11 and 60 °C. Activity at high temperature and high alkaline pH suggests suitability of the enzyme for its application in detergent industry.
Sreeja Chellappan - One of the best experts on this subject based on the ideXlab platform.
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Characterization of an extracellular alkaline serine protease from marine Engyodontium Album BTMFS10
Journal of Industrial Microbiology & Biotechnology, 2011Co-Authors: Sreeja Chellappan, Sarita,g Bhat, C. Jasmin, K. K. Elyas, Soorej M. Basheer, Archana Kishore, M. ChandrasekaranAbstract:An alkaline protease from marine Engyodontium Album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme. K _m, V _max, and K _cat of the enzyme were 4.727 × 10^−2 mg/ml, 394.68 U, and 4.2175 × 10^−2 s^−1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65°C), with maximum activity at pH 11 and 60°C. CaCl_2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65°C. Hg^2+, Cu^2+, Fe^3+, Zn^2+, Cd^+, and Al^3+ inhibited enzyme activity, while 1 mM Co^2+ enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications.
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Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium Album BTMFS10
World Journal of Microbiology and Biotechnology, 2010Co-Authors: C. Jasmin, Sreeja Chellappan, Sarita,g Bhat, Rajeev K. Sukumaran, K. K. Elyas, M. ChandrasekaranAbstract:An alkaline protease gene ( Eap ) was isolated for the first time from a marine fungus, Engyodontium Album . Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium Album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca^2+ binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein.
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Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium Album BTMFS10
'Springer Fachmedien Wiesbaden GmbH', 2010Co-Authors: Chandrasekaran M, Sreeja Chellappan, Jasmin C, Sarita,g Bhat, Rajeev, Sukumaran K, Elyas K KAbstract:An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium Album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium Album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca2? binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein.Cochin University of Science and TechnologyWorld J Microbiol Biotechnol (2010) 26:1269–127
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Characterization of an extracellular alkaline serine protease from marine Engyodontium Album BTMFS10
'Springer Fachmedien Wiesbaden GmbH', 2010Co-Authors: Chandrasekaran M, Sreeja Chellappan, Jasmin C, Soorej, Basheer M, Sarita,g Bhat, Archana Kishore, Elyas K KAbstract:An alkaline protease from marine Engyodontium Album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme.Km, Vmax, and Kcat of the enzyme were 4.727 9 10-2 mg/ml, 394.68 U, and 4.2175 9 10-2 s-1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65 C), withmaximumactivity at pH 11 and 60 C. CaCl2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65 C. Hg2?, Cu2?, Fe3?, Zn2?, Cd?, and Al3? inhibited enzyme activity, while 1 mMCo2? enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications.Cochin University of Science and TechnologyJ Ind Microbiol Biotechnol (2011) 38:743–752 DOI 10.1007/s10295-010-0914-
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production purification and partial characterization of a novel protease from marine Engyodontium Album btmfs10 under solid state fermentation
Process Biochemistry, 2006Co-Authors: Sreeja Chellappan, Sarita,g Bhat, C. Jasmin, K. K. Elyas, Soorej M. Basheer, M. ChandrasekaranAbstract:Engyodontium Album isolated from marine sediment produced protease, which was active at pH 11. Process parameters influencing the production of alkaline protease by marine E. Album was optimized. Particle size of <425 μm, 60% initial moisture content and incubation at 25 °C for 120 h were optimal for protease production under solid state fermentation (SSF) using wheat bran. The organism has two optimal pH (5 and 10) for maximal enzyme production. Sucrose as carbon source, ammonium hydrogen carbonate as additional inorganic nitrogen source and amino acid leucine enhanced enzyme production during SSF. The protease was purified and partially characterized. A 16-fold purified enzyme was obtained after ammonium sulphate precipitation and ion-exchange chromatography. Molecular weight of the purified enzyme protein was recorded approximately 38 kDa by SDS-PAGE. The enzyme showed maximum activity at pH 11 and 60 °C. Activity at high temperature and high alkaline pH suggests suitability of the enzyme for its application in detergent industry.
Jianming Chen - One of the best experts on this subject based on the ideXlab platform.
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secondary metabolites produced by the deep sea derived fungus Engyodontium Album
Chemistry of Natural Compounds, 2017Co-Authors: Weiyi Wang, Zhuo Chen, Yanyan Liao, Jianming ChenAbstract:Chemical investigation of the EtOH extract of a rice-fermented deep-sea-derived fungal strain, Engyodontium Album, led to the isolation of a new benzoic acid derivative, named Engyodontiumin A (1), together with four known compounds, 3,4-dihydroxybenzoic acid (2), 3-(2,4-dihydroxyphenyl) propionic acid (3), 3,4-dimethoxybenzoic acid (4), and trans-4-hydroxycinnamic acid (5). This strain was isolated from a marine sediment sample collected in the Atlantic Ocean (24°23′ W, 0°8′N, 3542 m depth). Their structures were elucidated by spectroscopic analyses, including 1H NMR, 13C NMR, 2D NMR (HSQC, HMBC, COSY), and HR-ESI-MS.
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two new benzoate derivatives and one new phenylacetate derivative from a marine derived fungus Engyodontium Album
Natural Product Research, 2017Co-Authors: Weiyi Wang, Ruixuan Chen, Zhuhua Luo, Wei Wang, Jianming ChenAbstract:Two new benzoate derivatives, ethyl 3,5-dimethoxy-2-propionylbenzoate (1) and ethyl 3,5-dihydroxy-2-propionylbenzoate (2), and one new phenylacetate derivative, ethyl 3,5-dimethoxy-2-propionylphenylacetate (3), together with 9 known compounds, were isolated from the fermentation of Engyodontium Album derived from deep sea sediment. Their structures were elucidated by spectroscopic techniques, such as NMR, IR and HRESIMS. Compound 3 exhibited inhibitory activities against methicillin-resistant Staphylococcus aureus ATCC 43300 (MRSA) and Vibrio vulnificus, with MIC values of 7.8 and 15.6 μg/mL, respectively.
Sarita,g Bhat - One of the best experts on this subject based on the ideXlab platform.
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Characterization of an extracellular alkaline serine protease from marine Engyodontium Album BTMFS10
Journal of Industrial Microbiology & Biotechnology, 2011Co-Authors: Sreeja Chellappan, Sarita,g Bhat, C. Jasmin, K. K. Elyas, Soorej M. Basheer, Archana Kishore, M. ChandrasekaranAbstract:An alkaline protease from marine Engyodontium Album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme. K _m, V _max, and K _cat of the enzyme were 4.727 × 10^−2 mg/ml, 394.68 U, and 4.2175 × 10^−2 s^−1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65°C), with maximum activity at pH 11 and 60°C. CaCl_2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65°C. Hg^2+, Cu^2+, Fe^3+, Zn^2+, Cd^+, and Al^3+ inhibited enzyme activity, while 1 mM Co^2+ enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications.
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Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium Album BTMFS10
World Journal of Microbiology and Biotechnology, 2010Co-Authors: C. Jasmin, Sreeja Chellappan, Sarita,g Bhat, Rajeev K. Sukumaran, K. K. Elyas, M. ChandrasekaranAbstract:An alkaline protease gene ( Eap ) was isolated for the first time from a marine fungus, Engyodontium Album . Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium Album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca^2+ binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein.
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Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium Album BTMFS10
'Springer Fachmedien Wiesbaden GmbH', 2010Co-Authors: Chandrasekaran M, Sreeja Chellappan, Jasmin C, Sarita,g Bhat, Rajeev, Sukumaran K, Elyas K KAbstract:An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium Album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium Album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca2? binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein.Cochin University of Science and TechnologyWorld J Microbiol Biotechnol (2010) 26:1269–127
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Characterization of an extracellular alkaline serine protease from marine Engyodontium Album BTMFS10
'Springer Fachmedien Wiesbaden GmbH', 2010Co-Authors: Chandrasekaran M, Sreeja Chellappan, Jasmin C, Soorej, Basheer M, Sarita,g Bhat, Archana Kishore, Elyas K KAbstract:An alkaline protease from marine Engyodontium Album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme.Km, Vmax, and Kcat of the enzyme were 4.727 9 10-2 mg/ml, 394.68 U, and 4.2175 9 10-2 s-1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65 C), withmaximumactivity at pH 11 and 60 C. CaCl2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65 C. Hg2?, Cu2?, Fe3?, Zn2?, Cd?, and Al3? inhibited enzyme activity, while 1 mMCo2? enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications.Cochin University of Science and TechnologyJ Ind Microbiol Biotechnol (2011) 38:743–752 DOI 10.1007/s10295-010-0914-
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production purification and partial characterization of a novel protease from marine Engyodontium Album btmfs10 under solid state fermentation
Process Biochemistry, 2006Co-Authors: Sreeja Chellappan, Sarita,g Bhat, C. Jasmin, K. K. Elyas, Soorej M. Basheer, M. ChandrasekaranAbstract:Engyodontium Album isolated from marine sediment produced protease, which was active at pH 11. Process parameters influencing the production of alkaline protease by marine E. Album was optimized. Particle size of <425 μm, 60% initial moisture content and incubation at 25 °C for 120 h were optimal for protease production under solid state fermentation (SSF) using wheat bran. The organism has two optimal pH (5 and 10) for maximal enzyme production. Sucrose as carbon source, ammonium hydrogen carbonate as additional inorganic nitrogen source and amino acid leucine enhanced enzyme production during SSF. The protease was purified and partially characterized. A 16-fold purified enzyme was obtained after ammonium sulphate precipitation and ion-exchange chromatography. Molecular weight of the purified enzyme protein was recorded approximately 38 kDa by SDS-PAGE. The enzyme showed maximum activity at pH 11 and 60 °C. Activity at high temperature and high alkaline pH suggests suitability of the enzyme for its application in detergent industry.
Shuhua Qi - One of the best experts on this subject based on the ideXlab platform.
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cytotoxic polyketides from the deep sea derived fungus Engyodontium Album dffscs021
Marine Drugs, 2014Co-Authors: Jie Wang, Xiaoyong Zhang, Xuhua Nong, Xinya Xu, Shuhua QiAbstract:Eight new chromones, Engyodontiumones A–H (1–8), and three new phenol derivatives (9–11) together with eight known polyketides (12–19) were isolated from the deep-sea-derived fungus Engyodontium Album DFFSCS021. Their structures were identified by extensive spectroscopic analysis. Compounds 8 and 16 showed significant selective cytotoxicity against human histiocytic lymphoma U937 cell line with IC50 values of 4.9 and 8.8 μM, respectively. In addition, this is the first time to report that 8, 15 and 16 had mild antibacterial activity against Escherichia coli and Bacillus subtilis, and 15 showed potent antilarval activity against barnacle Balanus amphitrite larval settlement.