Výsledky vyhledávání - "Iskandar, Dib"

Encapsulation ofTrigonopsis variabilisD-amino acid oxidase and fast comparison of the operational stabilities of free and immobilized preparations of the enzyme

Autor: Iskandar Dib, Jozef Nahálka, Bernd Nidetzky

Publikováno v: Biotechnology and Bioengineering. 99:251-260

A one-step procedure of immobilizing soluble and aggregated preparations of D-amino acid oxidase from Trigonopsis variabilis (TvDAO) is reported where carrier-free enzyme was entrapped in semipermeable microcapsules produced from the polycation poly(

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eaf6cf437ce55eb26f0c3f2f6da4943d
https://doi.org/10.1002/bit.21579

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Selective modification of surface-exposed thiol groups inTrigonopsis variabilisD-amino acid oxidase using poly(ethylene glycol) maleimide and its effect on activity and stability of the enzyme

Autor: Bernd Nidetzky, Anita Slavica, Iskandar Dib

Publikováno v: Biotechnology and Bioengineering. 96:9-17

Covalent modification of purified Trigonopsis variabilis D-amino acid oxidase using maleimide-activated poly(ethylene glycol) 5000 yielded a stable bioconjugate in which three surface-exposed cysteine side chains were selec- tively derivatized. Compa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a575bde5055b1f9f7bf1761fe06dd12f
https://doi.org/10.1002/bit.21181

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Trigonopsis variabilisd-Amino Acid Oxidase: Control of Protein Quality and Opportunities for Biocatalysis through Production inEscherichia coli

Autor: Bernd Nidetzky, Iskandar Dib, Damir Stanzer

Publikováno v: Applied and Environmental Microbiology. 73:331-333

Trigonopsis variabilisd-amino acid oxidase accounts for 35% ofEscherichia coliprotein when addedd-methionine suppresses the toxic activity of the recombinant product. PermeabilizedE. colicells are reusable and stabilized enzyme preparations. The puri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3882799eb9032dea988abe0e6af4a2b5
https://doi.org/10.1128/aem.01569-06

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Multiple factors determine the stability of D-amino acid oxidase from Trigonopsis variabilis

Autor: Iskandar, Dib, Slavica, Anita, Riethorst, Waander, Nidetzky, Bernd

Factors determining stability of D-amino acid oxidase form Trigonopsis variabilis were investigated.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=57a035e5b1ae::711b554dfbf107c1f955ea91760518d1
https://www.bib.irb.hr/632558

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Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences

Autor: Iskandar Dib, Anita Slavica, Bernd Nidetzky

One of the primary sources of enzyme instability is protein oxidative modification triggering activity loss or denaturation. We show here that the side chain of Cys108 is the main site undergoing stress-induced oxidation inTrigonopsis variabilisd-ami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65451aa5dc26ef481b0377080163be16
https://www.bib.irb.hr/350981

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The stabilizing effects of immobilization in D-amino acid oxidase from Trigonopsis variabilis

Autor: Iskandar Dib, Bernd Nidetzky

Publikováno v: BMC Biotechnology, Vol 8, Iss 1, p 72 (2008)
BMC Biotechnology

Background Immobilization of Trigonopsis variabilis D-amino acid oxidase (TvDAO) on solid support is the key to a reasonably stable performance of this enzyme in the industrial process for the conversion of cephalosporin C as well as in other biocata

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5a50f6a5fb6b2093219f2dd39dc01a7

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