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

Result code in 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>

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10511 - Environmental sciences (social aspects to be 5.7)

Project

<a href="/en/project/GAP105%2F11%2F0247" target="_blank" >GAP105/11/0247: Characterisation of algal organic matter and its effect on coagulation/flocculation process</a><br>

Continuities

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

Publication year

2012

Confidentiality

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

Name of the periodical

Water Research

ISSN

0043-1354

e-ISSN

—

Volume of the periodical

46

Issue of the periodical within the volume

17

Country of publishing house

GB - UNITED KINGDOM

Number of pages

8

Pages from-to

5583-5590

UT code for WoS article

000309297100013

EID of the result in the Scopus database

2-s2.0-84865956930