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The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli*.

Enzyme and microbial technology

Ignatova Z, Enfors S, Hobbie M, Taruttis S, Vogt C, Kasche V.
PMID: 10689073
Enzyme Microb Technol. 2000 Feb 01;26(2):165-170. doi: 10.1016/s0141-0229(99)00130-1.

Intracellular proteolysis is an important mechanism for regulating the level of the periplasmic enzyme penicillin amidase in Escherichia coli. Evidence is presented that the active enzyme is localized in the periplasmic space and maturation of pro-enzyme occurs during transport...

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Ignatova Z, Enfors S, Hobbie M, et al. The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli*. Enzyme Microb Technol. 2000;26(2):165-170doi: 10.1016/s0141-0229(99)00130-1.
Ignatova, Z., Enfors, S., Hobbie, M., Taruttis, S., Vogt, C., & Kasche, V. (2000). The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli*. Enzyme and microbial technology, 26(2), 165-170. https://doi.org/10.1016/s0141-0229(99)00130-1
Ignatova, et al. "The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli*." Enzyme and microbial technology vol. 26,2 (2000): 165-170. doi: https://doi.org/10.1016/s0141-0229(99)00130-1
Ignatova Z, Enfors S, Hobbie M, Taruttis S, Vogt C, Kasche V. The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli*. Enzyme Microb Technol. 2000 Feb 01;26(2):165-170. doi: 10.1016/s0141-0229(99)00130-1. PMID: 10689073.
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Improved penicillin amidase production using a genetically engineered mutant of Escherichia coli ATCC 11105.

Biotechnology and bioengineering

Robas N, Zouheiry H, Branlant G, Branlant C.
PMID: 18601241
Biotechnol Bioeng. 1993 Jan 05;41(1):14-24. doi: 10.1002/bit.260410104.

Penicillin G amidase (PGA) is a key enzyme for the industrial production of penicillin G derivatives used in therapeutics. Escherichia coli ATCC 11105 is the more commonly used strain for PGA production. To improve enzyme yield, we constructed various...

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Robas N, Zouheiry H, Branlant G, et al. Improved penicillin amidase production using a genetically engineered mutant of Escherichia coli ATCC 11105. Biotechnol Bioeng. 1993;41(1):14-24doi: 10.1002/bit.260410104.
Robas, N., Zouheiry, H., Branlant, G., & Branlant, C. (1993). Improved penicillin amidase production using a genetically engineered mutant of Escherichia coli ATCC 11105. Biotechnology and bioengineering, 41(1), 14-24. https://doi.org/10.1002/bit.260410104
Robas, N, et al. "Improved penicillin amidase production using a genetically engineered mutant of Escherichia coli ATCC 11105." Biotechnology and bioengineering vol. 41,1 (1993): 14-24. doi: https://doi.org/10.1002/bit.260410104
Robas N, Zouheiry H, Branlant G, Branlant C. Improved penicillin amidase production using a genetically engineered mutant of Escherichia coli ATCC 11105. Biotechnol Bioeng. 1993 Jan 05;41(1):14-24. doi: 10.1002/bit.260410104. PMID: 18601241.
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Enzyme catalyzed biotransformations in aqueous two-phase systems with precipitated substrate and/or product.

Biotechnology and bioengineering

Kasche V, Galunsky B.
PMID: 18623146
Biotechnol Bioeng. 1995 Feb 05;45(3):261-7. doi: 10.1002/bit.260450311.

Biotransformations catalyzed by free and immobilized enzymes have been carried out in aqueous suspensions with up to 25% (w/w) precipitated substrate or product. For the kinetically controlled synthesis of N-Acetyl-Tyr-Arg-NH(2) with up to 0.8 M insoluble activated substrate N-Acetyl-TyrOEt...

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Kasche V, Galunsky B. Enzyme catalyzed biotransformations in aqueous two-phase systems with precipitated substrate and/or product. Biotechnol Bioeng. 1995;45(3):261-7doi: 10.1002/bit.260450311.
Kasche, V., & Galunsky, B. (1995). Enzyme catalyzed biotransformations in aqueous two-phase systems with precipitated substrate and/or product. Biotechnology and bioengineering, 45(3), 261-7. https://doi.org/10.1002/bit.260450311
Kasche, V, and Galunsky, B. "Enzyme catalyzed biotransformations in aqueous two-phase systems with precipitated substrate and/or product." Biotechnology and bioengineering vol. 45,3 (1995): 261-7. doi: https://doi.org/10.1002/bit.260450311
Kasche V, Galunsky B. Enzyme catalyzed biotransformations in aqueous two-phase systems with precipitated substrate and/or product. Biotechnol Bioeng. 1995 Feb 05;45(3):261-7. doi: 10.1002/bit.260450311. PMID: 18623146.
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The production of 6-aminopenicillanic acid by a multistage tubular reactor packed with immobilized penicillin amidase.

Biotechnology and bioengineering

Park JM, Choi CY, Seong BL, Han MH.
PMID: 18546461
Biotechnol Bioeng. 1982 Jul;24(7):1623-37. doi: 10.1002/bit.260240714.

A theoretical model equation was derived to find the correlation between the conversion and the amount of immobilized penicillin amidase in column. The theoretical values of the conversion were predicted form this correlation and compared with experimental results. It...

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Park JM, Choi CY, Seong BL, et al. The production of 6-aminopenicillanic acid by a multistage tubular reactor packed with immobilized penicillin amidase. Biotechnol Bioeng. 1982;24(7):1623-37doi: 10.1002/bit.260240714.
Park, J. M., Choi, C. Y., Seong, B. L., & Han, M. H. (1982). The production of 6-aminopenicillanic acid by a multistage tubular reactor packed with immobilized penicillin amidase. Biotechnology and bioengineering, 24(7), 1623-37. https://doi.org/10.1002/bit.260240714
Park, J M, et al. "The production of 6-aminopenicillanic acid by a multistage tubular reactor packed with immobilized penicillin amidase." Biotechnology and bioengineering vol. 24,7 (1982): 1623-37. doi: https://doi.org/10.1002/bit.260240714
Park JM, Choi CY, Seong BL, Han MH. The production of 6-aminopenicillanic acid by a multistage tubular reactor packed with immobilized penicillin amidase. Biotechnol Bioeng. 1982 Jul;24(7):1623-37. doi: 10.1002/bit.260240714. PMID: 18546461.
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Effect of mass transfer in a recirculation batch reactor system for immobilized penicillin amidase.

Biotechnology and bioengineering

Park JM, Choi CY, Seong BL, Han MH.
PMID: 18546128
Biotechnol Bioeng. 1982 Oct;24(10):2215-26. doi: 10.1002/bit.260241008.

The effect of external mass transfer resistance on the overall reaction rate of the immobilized whole cell penicillin amidase of E. coli in a recirculation batch reactor was investigated. The internal diffusional resistance was found negligible as indicated by...

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Park JM, Choi CY, Seong BL, et al. Effect of mass transfer in a recirculation batch reactor system for immobilized penicillin amidase. Biotechnol Bioeng. 1982;24(10):2215-26doi: 10.1002/bit.260241008.
Park, J. M., Choi, C. Y., Seong, B. L., & Han, M. H. (1982). Effect of mass transfer in a recirculation batch reactor system for immobilized penicillin amidase. Biotechnology and bioengineering, 24(10), 2215-26. https://doi.org/10.1002/bit.260241008
Park, J M, et al. "Effect of mass transfer in a recirculation batch reactor system for immobilized penicillin amidase." Biotechnology and bioengineering vol. 24,10 (1982): 2215-26. doi: https://doi.org/10.1002/bit.260241008
Park JM, Choi CY, Seong BL, Han MH. Effect of mass transfer in a recirculation batch reactor system for immobilized penicillin amidase. Biotechnol Bioeng. 1982 Oct;24(10):2215-26. doi: 10.1002/bit.260241008. PMID: 18546128.
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Showing 1 to 5 of 5 entries