Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 548 entries
Sorted by: Best Match Show Resources per page
Enzymatic properties and expression patterns of five extracellular lipases of Fusarium graminearum in vitro.

Enzyme and microbial technology

Nguyen LN, Dao TT, Živković T, Fehrholz M, Schäfer W, Salomon S.
PMID: 25919623
Enzyme Microb Technol. 2010 May 05;46(6):479-86. doi: 10.1016/j.enzmictec.2010.02.005. Epub 2010 Feb 20.

Fusarium graminearum is a filamentous fungus that causes devastating diseases on plants of economic importance including maize, wheat, and barley. F. graminearum is able to utilize triglycerides as a carbon source during growth. Extracellular lipases are the preferred enzymes...

Cite
Nguyen LN, Dao TT, Živković T, et al. Enzymatic properties and expression patterns of five extracellular lipases of Fusarium graminearum in vitro. Enzyme Microb Technol. 2010;46(6):479-86doi: 10.1016/j.enzmictec.2010.02.005.
Nguyen, L. N., Dao, T. T., Živković, T., Fehrholz, M., Schäfer, W., & Salomon, S. (2010). Enzymatic properties and expression patterns of five extracellular lipases of Fusarium graminearum in vitro. Enzyme and microbial technology, 46(6), 479-86. https://doi.org/10.1016/j.enzmictec.2010.02.005
Nguyen, Long Nam, et al. "Enzymatic properties and expression patterns of five extracellular lipases of Fusarium graminearum in vitro." Enzyme and microbial technology vol. 46,6 (2010): 479-86. doi: https://doi.org/10.1016/j.enzmictec.2010.02.005
Nguyen LN, Dao TT, Živković T, Fehrholz M, Schäfer W, Salomon S. Enzymatic properties and expression patterns of five extracellular lipases of Fusarium graminearum in vitro. Enzyme Microb Technol. 2010 May 05;46(6):479-86. doi: 10.1016/j.enzmictec.2010.02.005. Epub 2010 Feb 20. PMID: 25919623.
Copy Download .nbib Format: NLM
Biological synthesis of platinum nanoparticles: Effect of initial metal concentration.

Enzyme and microbial technology

Riddin T, Gericke M, Whiteley CG.
PMID: 25919626
Enzyme Microb Technol. 2010 May 05;46(6):501-5. doi: 10.1016/j.enzmictec.2010.02.006. Epub 2010 Feb 19.

The unusual and novel properties of metal nanoparticles are highly sought after in a number of new and existing industries. Current chemical methods of nanoparticle synthesis have shown limited success and it is expected that the use of a...

Cite
Riddin T, Gericke M, Whiteley CG. Biological synthesis of platinum nanoparticles: Effect of initial metal concentration. Enzyme Microb Technol. 2010;46(6):501-5doi: 10.1016/j.enzmictec.2010.02.006.
Riddin, T., Gericke, M., & Whiteley, C. G. (2010). Biological synthesis of platinum nanoparticles: Effect of initial metal concentration. Enzyme and microbial technology, 46(6), 501-5. https://doi.org/10.1016/j.enzmictec.2010.02.006
Riddin, T, et al. "Biological synthesis of platinum nanoparticles: Effect of initial metal concentration." Enzyme and microbial technology vol. 46,6 (2010): 501-5. doi: https://doi.org/10.1016/j.enzmictec.2010.02.006
Riddin T, Gericke M, Whiteley CG. Biological synthesis of platinum nanoparticles: Effect of initial metal concentration. Enzyme Microb Technol. 2010 May 05;46(6):501-5. doi: 10.1016/j.enzmictec.2010.02.006. Epub 2010 Feb 19. PMID: 25919626.
Copy Download .nbib Format: NLM
Optimization of sodium dedecyl sulfate (SDS) addition coupled with adenosine triphosphate (ATP) regeneration for glutathione overproduction in high density cultivation of Candida utilis.

Enzyme and microbial technology

Liang G, Mo Y, Du G.
PMID: 25919630
Enzyme Microb Technol. 2010 May 05;46(6):526-33. doi: 10.1016/j.enzmictec.2010.02.007. Epub 2010 Feb 20.

In the previous study, glutathione production was elevated by adding precursor amino acids and adenosine triphosphate (ATP) in high cell density cultivation of Candida utilis. Furthermore, in the present research, glutathione production was further improved by optimizing sodium dedecyl...

Cite
Liang G, Mo Y, Du G. Optimization of sodium dedecyl sulfate (SDS) addition coupled with adenosine triphosphate (ATP) regeneration for glutathione overproduction in high density cultivation of Candida utilis. Enzyme Microb Technol. 2010;46(6):526-33doi: 10.1016/j.enzmictec.2010.02.007.
Liang, G., Mo, Y., & Du, G. (2010). Optimization of sodium dedecyl sulfate (SDS) addition coupled with adenosine triphosphate (ATP) regeneration for glutathione overproduction in high density cultivation of Candida utilis. Enzyme and microbial technology, 46(6), 526-33. https://doi.org/10.1016/j.enzmictec.2010.02.007
Liang, Guobin, et al. "Optimization of sodium dedecyl sulfate (SDS) addition coupled with adenosine triphosphate (ATP) regeneration for glutathione overproduction in high density cultivation of Candida utilis." Enzyme and microbial technology vol. 46,6 (2010): 526-33. doi: https://doi.org/10.1016/j.enzmictec.2010.02.007
Liang G, Mo Y, Du G. Optimization of sodium dedecyl sulfate (SDS) addition coupled with adenosine triphosphate (ATP) regeneration for glutathione overproduction in high density cultivation of Candida utilis. Enzyme Microb Technol. 2010 May 05;46(6):526-33. doi: 10.1016/j.enzmictec.2010.02.007. Epub 2010 Feb 20. PMID: 25919630.
Copy Download .nbib Format: NLM
Copper inducing effect on laccase production of white rot fungi native from Misiones (Argentina).

Enzyme and microbial technology

Fonseca MI, Shimizu E, Zapata PD, Villalba LL.
PMID: 25919631
Enzyme Microb Technol. 2010 May 05;46(6):534-9. doi: 10.1016/j.enzmictec.2009.12.017. Epub 2010 Jan 07.

Fungi may be selected as models for gene expression studies and further adaptation for biotechnological enzyme production. The aim of this work was to evaluate laccase production and to analyze the effect of Cu(2+) on selected fungi natives of...

Cite
Fonseca MI, Shimizu E, Zapata PD, et al. Copper inducing effect on laccase production of white rot fungi native from Misiones (Argentina). Enzyme Microb Technol. 2010;46(6):534-9doi: 10.1016/j.enzmictec.2009.12.017.
Fonseca, M. I., Shimizu, E., Zapata, P. D., & Villalba, L. L. (2010). Copper inducing effect on laccase production of white rot fungi native from Misiones (Argentina). Enzyme and microbial technology, 46(6), 534-9. https://doi.org/10.1016/j.enzmictec.2009.12.017
Fonseca, María I, et al. "Copper inducing effect on laccase production of white rot fungi native from Misiones (Argentina)." Enzyme and microbial technology vol. 46,6 (2010): 534-9. doi: https://doi.org/10.1016/j.enzmictec.2009.12.017
Fonseca MI, Shimizu E, Zapata PD, Villalba LL. Copper inducing effect on laccase production of white rot fungi native from Misiones (Argentina). Enzyme Microb Technol. 2010 May 05;46(6):534-9. doi: 10.1016/j.enzmictec.2009.12.017. Epub 2010 Jan 07. PMID: 25919631.
Copy Download .nbib Format: NLM
Cellobiose dehydrogenase-an extracellular fungal flavocytochrome.

Enzyme and microbial technology

Cameron MD, Aust SD.
PMID: 11166803
Enzyme Microb Technol. 2001 Feb 01;28(2):129-138. doi: 10.1016/s0141-0229(00)00307-0.

Wood-degrading fungi, including white-rot and soft-rot fungi as well as at least one brown-rot fungus, produce cellobiose dehydrogenase (CDH). CDH has generated recent interest because of its ability to facilitate the formation of free radicals and because it makes...

Cite
Cameron MD, Aust SD. Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Enzyme Microb Technol. 2001;28(2):129-138doi: 10.1016/s0141-0229(00)00307-0.
Cameron, M. D., & Aust, S. D. (2001). Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Enzyme and microbial technology, 28(2), 129-138. https://doi.org/10.1016/s0141-0229(00)00307-0
Cameron, M D., and Aust, S D.. "Cellobiose dehydrogenase-an extracellular fungal flavocytochrome." Enzyme and microbial technology vol. 28,2 (2001): 129-138. doi: https://doi.org/10.1016/s0141-0229(00)00307-0
Cameron MD, Aust SD. Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Enzyme Microb Technol. 2001 Feb 01;28(2):129-138. doi: 10.1016/s0141-0229(00)00307-0. PMID: 11166803.
Copy Download .nbib Format: NLM
Cell surface display of salmobin, a thrombin-like enzyme from Agkistrodon halys venom on Escherichia coli using ice nucleation protein.

Enzyme and microbial technology

Jeong H, Yoo S, Kim E.
PMID: 11166806
Enzyme Microb Technol. 2001 Feb 01;28(2):155-160. doi: 10.1016/s0141-0229(00)00315-x.

Cell surface display on Escherichia coli using ice nucleation protein was performed in order to develop a new expression system for recombinant eukaryotic proteins. Salmobin, the thrombin-like enzyme obtained from Korean snake (Agkistrodon halys) venom was displayed on the...

Cite
Jeong H, Yoo S, Kim E. Cell surface display of salmobin, a thrombin-like enzyme from Agkistrodon halys venom on Escherichia coli using ice nucleation protein. Enzyme Microb Technol. 2001;28(2):155-160doi: 10.1016/s0141-0229(00)00315-x.
Jeong, H., Yoo, S., & Kim, E. (2001). Cell surface display of salmobin, a thrombin-like enzyme from Agkistrodon halys venom on Escherichia coli using ice nucleation protein. Enzyme and microbial technology, 28(2), 155-160. https://doi.org/10.1016/s0141-0229(00)00315-x
Jeong, H -S., et al. "Cell surface display of salmobin, a thrombin-like enzyme from Agkistrodon halys venom on Escherichia coli using ice nucleation protein." Enzyme and microbial technology vol. 28,2 (2001): 155-160. doi: https://doi.org/10.1016/s0141-0229(00)00315-x
Jeong H, Yoo S, Kim E. Cell surface display of salmobin, a thrombin-like enzyme from Agkistrodon halys venom on Escherichia coli using ice nucleation protein. Enzyme Microb Technol. 2001 Feb 01;28(2):155-160. doi: 10.1016/s0141-0229(00)00315-x. PMID: 11166806.
Copy Download .nbib Format: NLM
Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization.

Enzyme and microbial technology

Guan YH, Lilley TH, Brook AH.
PMID: 11166815
Enzyme Microb Technol. 2001 Feb 01;28(2):218-224. doi: 10.1016/s0141-0229(00)00305-7.

A novel approach for the isolation and purification of penicillin acylase (PA), which couples aqueous two-phase partitioning and enzyme immobilization has been investigated.A PA yield of 90% was achieved by treating E. coli cells with 4% butyl acetate, freeze-thawing...

Cite
Guan YH, Lilley TH, Brook AH. Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization. Enzyme Microb Technol. 2001;28(2):218-224doi: 10.1016/s0141-0229(00)00305-7.
Guan, Y. H., Lilley, T. H., & Brook, A. H. (2001). Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization. Enzyme and microbial technology, 28(2), 218-224. https://doi.org/10.1016/s0141-0229(00)00305-7
Guan, Y H., et al. "Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization." Enzyme and microbial technology vol. 28,2 (2001): 218-224. doi: https://doi.org/10.1016/s0141-0229(00)00305-7
Guan YH, Lilley TH, Brook AH. Production of immobilized penicillin acylase using aqueous polymer systems for enzyme purification and in situ immobilization. Enzyme Microb Technol. 2001 Feb 01;28(2):218-224. doi: 10.1016/s0141-0229(00)00305-7. PMID: 11166815.
Copy Download .nbib Format: NLM
Large scale production of cyclohexanone monooxygenase from Escherichia coli TOP10 pQR239.

Enzyme and microbial technology

Doig SD, O'Sullivan LM, Patel S, Ward JM, Woodley JM.
PMID: 11166822
Enzyme Microb Technol. 2001 Feb 01;28(2):265-274. doi: 10.1016/s0141-0229(00)00320-3.

The cyclohexanone monooxygenase (CHMO) from Acinetobacter calcoaceticus NCIMB 9871 has been cloned into Escherichia coli in an L-arabinose inducible vector. The recombinant E. coli containing the L-arabinose inducible CHMO was grown at 1.5 litres under controlled conditions to determine...

Cite
Doig SD, O'Sullivan LM, Patel S, et al. Large scale production of cyclohexanone monooxygenase from Escherichia coli TOP10 pQR239. Enzyme Microb Technol. 2001;28(2):265-274doi: 10.1016/s0141-0229(00)00320-3.
Doig, S. D., O'Sullivan, L. M., Patel, S., Ward, J. M., & Woodley, J. M. (2001). Large scale production of cyclohexanone monooxygenase from Escherichia coli TOP10 pQR239. Enzyme and microbial technology, 28(2), 265-274. https://doi.org/10.1016/s0141-0229(00)00320-3
Doig, S D., et al. "Large scale production of cyclohexanone monooxygenase from Escherichia coli TOP10 pQR239." Enzyme and microbial technology vol. 28,2 (2001): 265-274. doi: https://doi.org/10.1016/s0141-0229(00)00320-3
Doig SD, O'Sullivan LM, Patel S, Ward JM, Woodley JM. Large scale production of cyclohexanone monooxygenase from Escherichia coli TOP10 pQR239. Enzyme Microb Technol. 2001 Feb 01;28(2):265-274. doi: 10.1016/s0141-0229(00)00320-3. PMID: 11166822.
Copy Download .nbib Format: NLM
Model-based bioreactor selection for large-scale solid-state cultivation of Coniothyrium minitans spores on oats.

Enzyme and microbial technology

Oostraa J, Tramper J, Rinzema A.
PMID: 11064047
Enzyme Microb Technol. 2000 Nov 15;27(9):652-663. doi: 10.1016/s0141-0229(00)00261-1.

Non-mixed and mixed SSF reactors were evaluated for their applicability in large-scale spore production of the biocontrol fungus Coniothyrium minitans. The major problem to overcome in large-scale SSF is heat accumulation. Testing various cooling strategies in large-scale bioreactors would...

Cite
Oostraa J, Tramper J, Rinzema A. Model-based bioreactor selection for large-scale solid-state cultivation of Coniothyrium minitans spores on oats. Enzyme Microb Technol. 2000;27(9):652-663doi: 10.1016/s0141-0229(00)00261-1.
Oostraa, J., Tramper, J., & Rinzema, A. (2000). Model-based bioreactor selection for large-scale solid-state cultivation of Coniothyrium minitans spores on oats. Enzyme and microbial technology, 27(9), 652-663. https://doi.org/10.1016/s0141-0229(00)00261-1
Oostraa, et al. "Model-based bioreactor selection for large-scale solid-state cultivation of Coniothyrium minitans spores on oats." Enzyme and microbial technology vol. 27,9 (2000): 652-663. doi: https://doi.org/10.1016/s0141-0229(00)00261-1
Oostraa J, Tramper J, Rinzema A. Model-based bioreactor selection for large-scale solid-state cultivation of Coniothyrium minitans spores on oats. Enzyme Microb Technol. 2000 Nov 15;27(9):652-663. doi: 10.1016/s0141-0229(00)00261-1. PMID: 11064047.
Copy Download .nbib Format: NLM
Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase. Solvent effects on cgtase.

Enzyme and microbial technology

Blackwood AD, Bucke C.
PMID: 11064053
Enzyme Microb Technol. 2000 Nov 15;27(9):704-708. doi: 10.1016/s0141-0229(00)00270-2.

Cyclodextrin glycosyltransferase (EC 2.4.1.19, CGTase) is an enzyme that produces cyclodextrins from starch via an intramolecular transglycosylation reaction. Addition of small amounts (10% v/v) of polar organic solvents can affect both the overall production yield and the type of...

Cite
Blackwood AD, Bucke C. Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase. Solvent effects on cgtase. Enzyme Microb Technol. 2000;27(9):704-708doi: 10.1016/s0141-0229(00)00270-2.
Blackwood, A. D., & Bucke, C. (2000). Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase. Solvent effects on cgtase. Enzyme and microbial technology, 27(9), 704-708. https://doi.org/10.1016/s0141-0229(00)00270-2
Blackwood, and Bucke. "Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase. Solvent effects on cgtase." Enzyme and microbial technology vol. 27,9 (2000): 704-708. doi: https://doi.org/10.1016/s0141-0229(00)00270-2
Blackwood AD, Bucke C. Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase. Solvent effects on cgtase. Enzyme Microb Technol. 2000 Nov 15;27(9):704-708. doi: 10.1016/s0141-0229(00)00270-2. PMID: 11064053.
Copy Download .nbib Format: NLM
Detection and substrate selectivity of new microbial D-amino acid oxidases.

Enzyme and microbial technology

Gabler M, Hensel M, Fischer L.
PMID: 11024524
Enzyme Microb Technol. 2000 Nov 01;27(8):605-611. doi: 10.1016/s0141-0229(00)00262-3.

In order to screen for new microbial D-amino acid oxidase activities a selective and sensitive peroxidase/o-dianisidine assay, detecting the formation of hydrogen peroxide was developed. Catalase, which coexists with oxidases in the peroxisomes or the microsomes and, which competes...

Cite
Gabler M, Hensel M, Fischer L. Detection and substrate selectivity of new microbial D-amino acid oxidases. Enzyme Microb Technol. 2000;27(8):605-611doi: 10.1016/s0141-0229(00)00262-3.
Gabler, M., Hensel, M., & Fischer, L. (2000). Detection and substrate selectivity of new microbial D-amino acid oxidases. Enzyme and microbial technology, 27(8), 605-611. https://doi.org/10.1016/s0141-0229(00)00262-3
Gabler, et al. "Detection and substrate selectivity of new microbial D-amino acid oxidases." Enzyme and microbial technology vol. 27,8 (2000): 605-611. doi: https://doi.org/10.1016/s0141-0229(00)00262-3
Gabler M, Hensel M, Fischer L. Detection and substrate selectivity of new microbial D-amino acid oxidases. Enzyme Microb Technol. 2000 Nov 01;27(8):605-611. doi: 10.1016/s0141-0229(00)00262-3. PMID: 11024524.
Copy Download .nbib Format: NLM
Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism.

Enzyme and microbial technology

Aymard C, Belarbi A.
PMID: 11024525
Enzyme Microb Technol. 2000 Nov 01;27(8):612-618. doi: 10.1016/s0141-0229(00)00258-1.

Heat induced enzyme inactivation or protein denaturation is now well documented, due to progresses in methods, instruments and computation resources. Complex mechanisms, rather than the classic simple "one step - two states" model (still in use) are recognized in...

Cite
Aymard C, Belarbi A. Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzyme Microb Technol. 2000;27(8):612-618doi: 10.1016/s0141-0229(00)00258-1.
Aymard, C., & Belarbi, A. (2000). Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzyme and microbial technology, 27(8), 612-618. https://doi.org/10.1016/s0141-0229(00)00258-1
Aymard, and Belarbi. "Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism." Enzyme and microbial technology vol. 27,8 (2000): 612-618. doi: https://doi.org/10.1016/s0141-0229(00)00258-1
Aymard C, Belarbi A. Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzyme Microb Technol. 2000 Nov 01;27(8):612-618. doi: 10.1016/s0141-0229(00)00258-1. PMID: 11024525.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 548 entries