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The effect of peptides and proteins from cyanobacterium Microcystis aeruginosa on coagulation of kaolin particles
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SYSNO ASEP 0378897 Druh ASEP C - Konferenční příspěvek (mezinárodní konf.) Zařazení RIV Záznam nebyl označen do RIV Název The effect of peptides and proteins from cyanobacterium Microcystis aeruginosa on coagulation of kaolin particles Tvůrce(i) Šafaříková, Jana (UH-J) RID
Pivokonský, Martin (UH-J) SAI, ORCID, RIDZdroj.dok. Proceedings of the 6th IWA International Conference for Young Water Professionals. - Budapest : IWA, 2012 Rozsah stran iwa-9893 Poč.str. 7 s. Forma vydání CD-ROM - CD-ROM Akce IWA International Conference for Young Water Professionals /6./ (IWA YWPC 2012) Datum konání 10.07.2012-13.07.2012 Místo konání Budapest Země HU - Maďarsko Typ akce WRD Jazyk dok. eng - angličtina Země vyd. HU - Maďarsko Klíč. slova algal organic matter (AOM) ; coagulation ; complexes formation ; peptides/proteins Vědní obor RIV BK - Mechanika tekutin CEP GAP105/11/0247 GA ČR - Grantová agentura ČR CEZ AV0Z20600510 - UH-J (2005-2011) Anotace In this study, the coagulation of peptides and proteins produced by cyanobacterium Microcystis aeruginosa and their influence on the coagulation of hydrophobic kaolin particles were investigated. For this purpose, the dosage of ferric sulphate used as coagulant was optimized and jar tests with kaolin, peptides/proteins and both kaolin and peptides/proteins were carried out under different pH conditions. At pH 4 – 5.5 the efficient coagulation of peptides/proteins took place and peptides/proteins were also found to contribute to the coagulation of kaolin particles at this pH. Charge neutralization and adsorption were found to be dominant coagulation mechanisms. The coagulation efficiency and the character of the prevailing coagulation mechanism were strongly dependent on charge characteristics of peptides/proteins, kaolin and hydrolysis products of iron used as coagulation agent. At pH about 6, the coagulation process was deteriorated by the formation of soluble Fe-peptide/protein complexes. Through affinity chromatography analysis it was demonstrated that peptides/proteins able to form complexes with iron are of MW 52, 10, 8.4, 7.7, 6.5, 2.8 and 1 kDa. Pracoviště Ústav pro hydrodynamiku Kontakt Soňa Hnilicová, hnilicova@ih.cas.cz, Tel.: 233 109 003 Rok sběru 2013
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