Biosorpce Cd2+ and Zn2+ buňkami Saccharomyces cerevisiae s modifikovaným buněčným povrchem.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F08%3A00019923" target="_blank" >RIV/60461373:22330/08:00019923 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Biosorption of Cd2+ and Zn2+ by cell surface-engineered Saccharomyces cerevisiae.

Popis výsledku v původním jazyce

The carboxyl-terminal part of sexual adhesion glycoprotein -agglutinin (AG1Cp) was employed as an anchoring domain for surface display of short metal binding peptides of sequences N-Ser-(Gly-Cys-Gly-Cys-Pro-Cys-Gly-Cys)2-Gly-C (CP2 peptide) and N-Ser-(Gly-His-His-Pro-His)3-Gly-C (HP3 peptide) in the cell wall of potential biosorbent Saccharomyces cerevisiae. The constructed genetic fusions were efficiently expressed and found covalently attached to cell wall glucan and both O- and N-glycosylated. As a consequence of AG1Cp over-expression the nitrogen content of cell wall increased by 30%, which was reflected by increased sorption capacity of both isolated cell walls and intact cells. Comparing to parental cells, the surface display of mere anchoring domain doubled the amount of Cd2+ and Zn2+ adsorbed by modified biomass from solutions containing 10 to 200 M metal ions. Displayed CP2 and HP3 sequences showed selectivity towards Cd2+ and Zn2+, respectively. The fusion of CP2 peptide to A

Název v anglickém jazyce

Biosorption of Cd2+ and Zn2+ by cell surface-engineered Saccharomyces cerevisiae.

Popis výsledku anglicky

The carboxyl-terminal part of sexual adhesion glycoprotein -agglutinin (AG1Cp) was employed as an anchoring domain for surface display of short metal binding peptides of sequences N-Ser-(Gly-Cys-Gly-Cys-Pro-Cys-Gly-Cys)2-Gly-C (CP2 peptide) and N-Ser-(Gly-His-His-Pro-His)3-Gly-C (HP3 peptide) in the cell wall of potential biosorbent Saccharomyces cerevisiae. The constructed genetic fusions were efficiently expressed and found covalently attached to cell wall glucan and both O- and N-glycosylated. As a consequence of AG1Cp over-expression the nitrogen content of cell wall increased by 30%, which was reflected by increased sorption capacity of both isolated cell walls and intact cells. Comparing to parental cells, the surface display of mere anchoring domain doubled the amount of Cd2+ and Zn2+ adsorbed by modified biomass from solutions containing 10 to 200 M metal ions. Displayed CP2 and HP3 sequences showed selectivity towards Cd2+ and Zn2+, respectively. The fusion of CP2 peptide to A

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

International Biodeterioration and Biodegradation

ISSN

0964-8305

e-ISSN

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Svazek periodika

2008

Číslo periodika v rámci svazku

60

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

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Kód UT WoS článku

000249110100005

EID výsledku v databázi Scopus

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