Acidic Versus Alkaline Bacterial Degradation of Lignin Through Engineered Strain E. coli BL21(Lacc): Exploring the Differences in Chemical Structure, Morphology, and Degradation Products
There is increasing interest in research on biodegradation of lignin compounds as potential building blocks in applications related to renewable products. More attention is needed to evaluate the impact of the initial pH conditions for bacterial degradation of lignin. In this study, we conducted experiments on biodegradation of lignin in acidic and mild alkaline conditions. Biodegradation acid, lignin is chemically pretreated with hydrogen peroxide. alkaline biodegradation achieved by developing the growth of bacteria on Luria and Bertani medium with alkali lignin as the sole carbon source.
Mutant strains of Escherichia coli BL21 (Lacc) is used to carry out the biodegradation of lignin during 10 days of incubation. The results show that under acidic conditions the dominance of aliphatic compounds from C3-C4 species. Alkaline biodegradation produced in the context of oxidative stress, with a larger number of aryl compounds. The final pH value of acid and alkaline biodegradation of lignin were 2.53 and 7.90, respectively. The results of gas chromatography mass spectrometry analysis detected compounds such as crotonic acid, lactic acid and 3-hydroxybutanoic acid for acid conditions, with potential applications for adhesives and polymer precursors.
In alkaline conditions, the compounds detected include 2-phenylethanol and dehydroabietic acid, with potential applications for fragrances and tumor / anti-anti-inflammatory drugs. Size-exclusion chromatography analysis showed that the average molecular weight of alkali lignin biodegradation increased 6.75-fold compared with the acid method, resulting in repolymerization of the molecular structure. Lignin repolymerization coincided with an increase in relative abundance and alcohol isovanillyl dehydroabietic acid, of 2.70 and 3.96% on the day zero to 13.43 and 10.26% on the 10th day.
The results of Fourier-transformed infrared spectroscopy to detect the presence of C = O bonds and OH functional groups associated with the carboxylic acid in acid method. In the alkaline method is no greater preponderance of signals associated with the aromatic framework structure, the amine functional group and a C – O – bonds. Lignin biodegradation product of E. coli BL21 (laccase), under the condition of different initial pH, shows promising potential to enlarge the spectrum of renewable products for biorefinery activities.
Acidic Versus Alkaline Bacterial Degradation of Lignin Through Engineered Strain E. coli BL21(Lacc): Exploring the Differences in Chemical Structure, Morphology, and Degradation Products
Evaluating the Effect of azole antifungal agents on Stress Response and nano Surface properties anthropi Ochrobactrum Aspcl2.2
Azole antifungal molecules are widely used as active ingredients in various products, such as pharmaceuticals and pesticides. This prompted their release into the natural environment. The detailed mechanism of their effect on natural ecosystems biotic components remain unexplored. Our research aims to test the response of Ochrobactrum anthropi AspCl2.2 with the presence of four azole antifungal agents (clotrimazole, fluconazole, climbazole, epoxiconazole).
Experiments conducted on the analysis of cell metabolic activity, cell membrane permeability, the level of total glutathione and glutathione S-transferase activity. This study allows for the evaluation of the oxidative stress response of cells to the presence of azole antifungals. In addition, changes in the surface properties of nanomaterials, including adhesive and elastic features of the cells, were investigated using atomic force microscopy (AFM) and spectrophotometric methods.
Description: Caspase-9 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFα, TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues.
Description: Caspase-9 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFα, TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues.
Description: Caspase-9 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFα, TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues.
Description: Caspase-9 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFα, TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues.
Description: Caspase 9 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspase APAF1; this step is thought to be one of the earliest in the caspase activation cascade.
Description: Caspase 9 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspase APAF1; this step is thought to be one of the earliest in the caspase activation cascade.
Description: Caspase 9 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspase APAF1; this step is thought to be one of the earliest in the caspase activation cascade.
Description: Caspase 9 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspase APAF1; this step is thought to be one of the earliest in the caspase activation cascade.
Description: Caspase-9, also called APAF3, is an initiator caspase, encoded by the CASP9 gene. The gene is mapped to chromosome 1p36.3-p36.1 by FISH. CASP9 is identified as a member of the caspase family that participates in CASP3 activation in vitro. And it also regarded as the most upstream member of the apoptotic protease cascade that is triggered by Cytochrome C and dATP. The crystal structure of CASP9 is complex with the BIR3 in an inhibitory domain of XIAP at 2.4-angstrom resolution and the gene contains 9 exons and spans approximately 35 kb of genomic DNA. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of Cytochrome C and dATP, an event that leads to CASP9 activation. Activity increases dramatically upon association with the apoptosome complex. And the majority of CASP9 knockout mice died perinatally with a markedly enlarged and malformed cerebrum caused by reduced apoptosis during brain development.
Description: Caspase-9 is also known as MCH6 or APAF3. The CASP9 gene encodes a member of the cysteine-aspartic acid protease family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex ofCytochrome Cand the Apoptotic peptidase activating factor 1. This step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants.
Description: CASP9 is also known as MCH6 or APAF3. This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants.
Description: CASP9 is also known as MCH6 or APAF3. This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants.
The results indicate that oxidative stress promotes bacterial azoles. The strongest difference recorded for cells cultivated with fluconazole. The most toxic effects have been associated with climbazole.
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