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Francois K Mulenga - One of the best experts on this subject based on the ideXlab platform.
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sensitivity analysis of austin s scale up model for tumbling ball mills part 2 effects of full scale milling parameters
Powder Technology, 2017Co-Authors: Francois K MulengaAbstract:Abstract The need for scale-up of laboratory milling data to full operation is critical especially for the proper selection of design parameters. This paper investigates the extent to which full-scale milling conditions and design parameters influence the discharged product. Austin's scale-up procedure for batch grinding data is used to this end and is applied to a continuous mill operated in open circuit. The circuit was simulated in steady-state regime using randomly generated parameters within predefined ranges. These enabled the iterative computation of the corresponding mill products, average characteristic sizes and standard deviations. Simulation outcomes suggest that mill diameter, top-up ball diameter, in-mill flow pattern, and two scale-up correction factors in Austin's model have a greater bearing on mill product. The two correction factors account for the change in mill diameter and ball size from batch to full-scale milling respectively.
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sensitivity analysis of austin s scale up model for tumbling ball mills part 1 effects of batch grinding parameters
Powder Technology, 2017Co-Authors: Francois K MulengaAbstract:Abstract It is often desirable to predict with confidence the performance of a full-scale mill using good quality laboratory data. In the present paper, the sensitivity of Austin's scale-up procedure to batch grinding data was investigated. To this end, the effects of breakage function and selection function parameters on the product of a full-scale mill in open circuit were simulated. An array of numbers was randomly generated around the average value of the batch milling parameter considered and within a predefined range. Then, the mill products corresponding to the array of values were calculated. After analysis, Austin's scale-up model was found to be more sensitive to the selection function than the breakage function. Selection function parameters should therefore be measured with great care when modelling open mill circuits.
Thiago Henrique Napoleao - One of the best experts on this subject based on the ideXlab platform.
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binding targets of termiticidal lectins from the bark and leaf of myracrodruon urundeuva in the gut of nasutitermes corniger workers
Pest Management Science, 2018Co-Authors: Thâmarah De Albuquerque Lima, Leonardo Prezzi Dornelles, Ana Patricia Silva De Oliveira, Caio Cs Guedes, Sueden O Souza, Russolina B Zingali, Thiago Henrique Napoleao, Patricia Mg PaivaAbstract:BACKGROUND Lectins, carbohydrate-binding proteins, from the bark (MuBL) and leaf (Mull) of Myracrodruon urundeuva are termiticidal agents against Nasutitermes corniger workers and have been shown to induce oxidative stress and cell death in the midgut of these insects. In this study, we investigated the binding targets of MuBL and Mull in the gut of N. corniger workers by determining the effects of these lectins on the activity of digestive enzymes. In addition, we used mass spectrometry to identify peptides from gut proteins that adsorbed to MuBL-Sepharose and Mull-Sepharose columns. RESULTS Exoglucanase activity was neutralized in the presence of MuBL and stimulated by Mull. α-l-Arabinofuranosidase activity was not affected by MuBL but was inhibited by Mull. Both lectins stimulated α-amylase activity and inhibited protease and trypsin-like activities. Peptides with homology to apolipophorin, trypsin-like enzyme, and ABC transporter substrate-binding protein were detected from proteins that adsorbed to MuBL-Sepharose, while peptides from proteins that bound to Mull-Sepharose shared homology with apolipophorin. CONCLUSION This study revealed that digestive enzymes and transport proteins found in worker guts can be recognized by MuBL and Mull. Thus, the mechanism of their termiticidal activity may involve changes in the digestion and absorption of nutrients. © 2018 Society of Chemical Industry.
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termiticidal activity of lectins from myracrodruon urundeuva against nasutitermes corniger and its mechanisms
International Biodeterioration & Biodegradation, 2011Co-Authors: Thiago Henrique Napoleao, Thâmarah De Albuquerque Lima, Francis Soares Gomes, Nataly Diniz De Lima Santos, Auristela C Albuquerque, Luana C B B Coelho, Patricia Maria Guedes PaivaAbstract:Abstract The isolation of lectins from Myracrodruon urundeuva bark (MuBL) and heartwood (MuHL) as well as the termiticidal activity of MuHL against Nasutitermes corniger has already been described. This work reports on the purification of a leaf lectin (Mull) and the characterization of MuBL, MuHL, and Mull; also described are the resistance of hemagglutinating activity of the three lectins to trypsin activity from N. corniger gut and the termiticidal activity on N. corniger of MuBL (LC50 of 0.974 mg ml−1 on workers and 0.787 mg ml−1 on soldiers) and Mull (LC50 of 0.374 mg ml−1 on workers and 0.432 mg ml−1 on soldiers). The antibacterial effect of MuBL, MuHL, and Mull on bacteria from gut of N. corniger was also investigated and lectins showed similar bacteriostatic activity (MIC of 62.5 μg ml−1 for workers and 125 μg ml−1 for soldiers). MuBL and MuHL were more efficient bactericidal agents on bacteria in the workers’ gut (MBC of 125 μg ml−1) than Mull (MBC of 250 μg ml−1) and similar bactericidal activity was detected on bacteria in the gut of soldiers (MBC of 250 μg ml−1). The termiticidal activity of M. urundeuva lectins can be explained by the chitin-binding property, resistance to termite digestive enzyme, and the antibacterial effect on symbiotic bacteria of N. corniger gut.
Thâmarah De Albuquerque Lima - One of the best experts on this subject based on the ideXlab platform.
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binding targets of termiticidal lectins from the bark and leaf of myracrodruon urundeuva in the gut of nasutitermes corniger workers
Pest Management Science, 2018Co-Authors: Thâmarah De Albuquerque Lima, Leonardo Prezzi Dornelles, Ana Patricia Silva De Oliveira, Caio Cs Guedes, Sueden O Souza, Russolina B Zingali, Thiago Henrique Napoleao, Patricia Mg PaivaAbstract:BACKGROUND Lectins, carbohydrate-binding proteins, from the bark (MuBL) and leaf (Mull) of Myracrodruon urundeuva are termiticidal agents against Nasutitermes corniger workers and have been shown to induce oxidative stress and cell death in the midgut of these insects. In this study, we investigated the binding targets of MuBL and Mull in the gut of N. corniger workers by determining the effects of these lectins on the activity of digestive enzymes. In addition, we used mass spectrometry to identify peptides from gut proteins that adsorbed to MuBL-Sepharose and Mull-Sepharose columns. RESULTS Exoglucanase activity was neutralized in the presence of MuBL and stimulated by Mull. α-l-Arabinofuranosidase activity was not affected by MuBL but was inhibited by Mull. Both lectins stimulated α-amylase activity and inhibited protease and trypsin-like activities. Peptides with homology to apolipophorin, trypsin-like enzyme, and ABC transporter substrate-binding protein were detected from proteins that adsorbed to MuBL-Sepharose, while peptides from proteins that bound to Mull-Sepharose shared homology with apolipophorin. CONCLUSION This study revealed that digestive enzymes and transport proteins found in worker guts can be recognized by MuBL and Mull. Thus, the mechanism of their termiticidal activity may involve changes in the digestion and absorption of nutrients. © 2018 Society of Chemical Industry.
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termiticidal activity of lectins from myracrodruon urundeuva against nasutitermes corniger and its mechanisms
International Biodeterioration & Biodegradation, 2011Co-Authors: Thiago Henrique Napoleao, Thâmarah De Albuquerque Lima, Francis Soares Gomes, Nataly Diniz De Lima Santos, Auristela C Albuquerque, Luana C B B Coelho, Patricia Maria Guedes PaivaAbstract:Abstract The isolation of lectins from Myracrodruon urundeuva bark (MuBL) and heartwood (MuHL) as well as the termiticidal activity of MuHL against Nasutitermes corniger has already been described. This work reports on the purification of a leaf lectin (Mull) and the characterization of MuBL, MuHL, and Mull; also described are the resistance of hemagglutinating activity of the three lectins to trypsin activity from N. corniger gut and the termiticidal activity on N. corniger of MuBL (LC50 of 0.974 mg ml−1 on workers and 0.787 mg ml−1 on soldiers) and Mull (LC50 of 0.374 mg ml−1 on workers and 0.432 mg ml−1 on soldiers). The antibacterial effect of MuBL, MuHL, and Mull on bacteria from gut of N. corniger was also investigated and lectins showed similar bacteriostatic activity (MIC of 62.5 μg ml−1 for workers and 125 μg ml−1 for soldiers). MuBL and MuHL were more efficient bactericidal agents on bacteria in the workers’ gut (MBC of 125 μg ml−1) than Mull (MBC of 250 μg ml−1) and similar bactericidal activity was detected on bacteria in the gut of soldiers (MBC of 250 μg ml−1). The termiticidal activity of M. urundeuva lectins can be explained by the chitin-binding property, resistance to termite digestive enzyme, and the antibacterial effect on symbiotic bacteria of N. corniger gut.
Patricia Maria Guedes Paiva - One of the best experts on this subject based on the ideXlab platform.
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termiticidal activity of lectins from myracrodruon urundeuva against nasutitermes corniger and its mechanisms
International Biodeterioration & Biodegradation, 2011Co-Authors: Thiago Henrique Napoleao, Thâmarah De Albuquerque Lima, Francis Soares Gomes, Nataly Diniz De Lima Santos, Auristela C Albuquerque, Luana C B B Coelho, Patricia Maria Guedes PaivaAbstract:Abstract The isolation of lectins from Myracrodruon urundeuva bark (MuBL) and heartwood (MuHL) as well as the termiticidal activity of MuHL against Nasutitermes corniger has already been described. This work reports on the purification of a leaf lectin (Mull) and the characterization of MuBL, MuHL, and Mull; also described are the resistance of hemagglutinating activity of the three lectins to trypsin activity from N. corniger gut and the termiticidal activity on N. corniger of MuBL (LC50 of 0.974 mg ml−1 on workers and 0.787 mg ml−1 on soldiers) and Mull (LC50 of 0.374 mg ml−1 on workers and 0.432 mg ml−1 on soldiers). The antibacterial effect of MuBL, MuHL, and Mull on bacteria from gut of N. corniger was also investigated and lectins showed similar bacteriostatic activity (MIC of 62.5 μg ml−1 for workers and 125 μg ml−1 for soldiers). MuBL and MuHL were more efficient bactericidal agents on bacteria in the workers’ gut (MBC of 125 μg ml−1) than Mull (MBC of 250 μg ml−1) and similar bactericidal activity was detected on bacteria in the gut of soldiers (MBC of 250 μg ml−1). The termiticidal activity of M. urundeuva lectins can be explained by the chitin-binding property, resistance to termite digestive enzyme, and the antibacterial effect on symbiotic bacteria of N. corniger gut.
Patricia Mg Paiva - One of the best experts on this subject based on the ideXlab platform.
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binding targets of termiticidal lectins from the bark and leaf of myracrodruon urundeuva in the gut of nasutitermes corniger workers
Pest Management Science, 2018Co-Authors: Thâmarah De Albuquerque Lima, Leonardo Prezzi Dornelles, Ana Patricia Silva De Oliveira, Caio Cs Guedes, Sueden O Souza, Russolina B Zingali, Thiago Henrique Napoleao, Patricia Mg PaivaAbstract:BACKGROUND Lectins, carbohydrate-binding proteins, from the bark (MuBL) and leaf (Mull) of Myracrodruon urundeuva are termiticidal agents against Nasutitermes corniger workers and have been shown to induce oxidative stress and cell death in the midgut of these insects. In this study, we investigated the binding targets of MuBL and Mull in the gut of N. corniger workers by determining the effects of these lectins on the activity of digestive enzymes. In addition, we used mass spectrometry to identify peptides from gut proteins that adsorbed to MuBL-Sepharose and Mull-Sepharose columns. RESULTS Exoglucanase activity was neutralized in the presence of MuBL and stimulated by Mull. α-l-Arabinofuranosidase activity was not affected by MuBL but was inhibited by Mull. Both lectins stimulated α-amylase activity and inhibited protease and trypsin-like activities. Peptides with homology to apolipophorin, trypsin-like enzyme, and ABC transporter substrate-binding protein were detected from proteins that adsorbed to MuBL-Sepharose, while peptides from proteins that bound to Mull-Sepharose shared homology with apolipophorin. CONCLUSION This study revealed that digestive enzymes and transport proteins found in worker guts can be recognized by MuBL and Mull. Thus, the mechanism of their termiticidal activity may involve changes in the digestion and absorption of nutrients. © 2018 Society of Chemical Industry.
