Coagulation of peptides and proteins produced by Microcystis aeruginosa: Interaction mechanisms and the effect of Fe-peptide/protein complexes formation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985874%3A_____%2F12%3A00380327" target="_blank" >RIV/67985874:_____/12:00380327 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0043135412005349?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0043135412005349?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.watres.2012.07.040" target="_blank" >10.1016/j.watres.2012.07.040</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Coagulation of peptides and proteins produced by Microcystis aeruginosa: Interaction mechanisms and the effect of Fe-peptide/protein complexes formation

Popis výsledku v původním jazyce

This paper focuses on elucidation of the mechanisms involved in the coagulation of peptides and proteins contained in cellular organic matter (COM) of cyanobacterium Microcystis aeruginosa by ferric coagulant. Furthermore, coagulation inhibition due to the formation of Fe-peptide/protein surface complexes was evaluated. The results of coagulation testing imply that removability of peptides and proteins is highly dependent on pH value which determines charge characteristics of coagulation system compounds and therefore the mechanisms of interactions between them. The highest peptide/protein removal was obtained in the pH range of 4-6 owing to charge neutralization of peptide/protein negative surface by positively charged hydrolysis products of ferric coagulant. At low COM/Fe ratio (COM/Fe <0.33), adsorption of peptides/proteins onto ferric oxide-hydroxide particles, described as electrostatic patch model, enables the coagulation at pH 6-8. On the contrary, steric stabilization reduces coagulation at pH 6-8 if the ratio COM/Fe is high (COM/Fe >0.33). Coagulation of peptides and proteins is disturbed at pH 6-7 as a consequence of Fe-peptide/protein complexes formation. The maximum ability of peptides/proteins to form soluble complexes with Fe was found just at pH 6, when peptides/proteins bind 1.38 mmol Fe per 1 g of peptide/protein DOC. Complex forming peptides and proteins of relative molecular weights of 1, 2.8, 6, 8, 8.5, 10 and 52 kDa were isolated by affinity chromatography. (C) 2012 Elsevier Ltd. All rights reserved.

Název v anglickém jazyce

Coagulation of peptides and proteins produced by Microcystis aeruginosa: Interaction mechanisms and the effect of Fe-peptide/protein complexes formation

Popis výsledku anglicky

This paper focuses on elucidation of the mechanisms involved in the coagulation of peptides and proteins contained in cellular organic matter (COM) of cyanobacterium Microcystis aeruginosa by ferric coagulant. Furthermore, coagulation inhibition due to the formation of Fe-peptide/protein surface complexes was evaluated. The results of coagulation testing imply that removability of peptides and proteins is highly dependent on pH value which determines charge characteristics of coagulation system compounds and therefore the mechanisms of interactions between them. The highest peptide/protein removal was obtained in the pH range of 4-6 owing to charge neutralization of peptide/protein negative surface by positively charged hydrolysis products of ferric coagulant. At low COM/Fe ratio (COM/Fe <0.33), adsorption of peptides/proteins onto ferric oxide-hydroxide particles, described as electrostatic patch model, enables the coagulation at pH 6-8. On the contrary, steric stabilization reduces coagulation at pH 6-8 if the ratio COM/Fe is high (COM/Fe >0.33). Coagulation of peptides and proteins is disturbed at pH 6-7 as a consequence of Fe-peptide/protein complexes formation. The maximum ability of peptides/proteins to form soluble complexes with Fe was found just at pH 6, when peptides/proteins bind 1.38 mmol Fe per 1 g of peptide/protein DOC. Complex forming peptides and proteins of relative molecular weights of 1, 2.8, 6, 8, 8.5, 10 and 52 kDa were isolated by affinity chromatography. (C) 2012 Elsevier Ltd. All rights reserved.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10511 - Environmental sciences (social aspects to be 5.7)

Projekt

<a href="/cs/project/GAP105%2F11%2F0247" target="_blank" >GAP105/11/0247: Charakterizace organických látek produkovaných sinicemi a řasami a jejich vliv na koagulaci a flokulaci</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Water Research

ISSN

0043-1354

e-ISSN

—

Svazek periodika

46

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

5583-5590

Kód UT WoS článku

000309297100013

EID výsledku v databázi Scopus

2-s2.0-84865956930