Number of the records: 1
The effect of peptides and proteins from cyanobacterium Microcystis aeruginosa on coagulation of kaolin particles
- 1.
SYSNO ASEP 0378897 Document Type C - Proceedings Paper (int. conf.) R&D Document Type The record was not marked in the RIV Title The effect of peptides and proteins from cyanobacterium Microcystis aeruginosa on coagulation of kaolin particles Author(s) Šafaříková, Jana (UH-J) RID
Pivokonský, Martin (UH-J) SAI, ORCID, RIDSource Title Proceedings of the 6th IWA International Conference for Young Water Professionals. - Budapest : IWA, 2012 Pages iwa-9893 Number of pages 7 s. Publication form CD-ROM - CD-ROM Action IWA International Conference for Young Water Professionals /6./ (IWA YWPC 2012) Event date 10.07.2012-13.07.2012 VEvent location Budapest Country HU - Hungary Event type WRD Language eng - English Country HU - Hungary Keywords algal organic matter (AOM) ; coagulation ; complexes formation ; peptides/proteins Subject RIV BK - Fluid Dynamics R&D Projects GAP105/11/0247 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z20600510 - UH-J (2005-2011) Annotation 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. Workplace Institute of Hydrodynamics Contact Soňa Hnilicová, hnilicova@ih.cas.cz, Tel.: 233 109 003 Year of Publishing 2013
Number of the records: 1