AI Article Synopsis

  • - This paper investigates extracellular polymeric substances (EPS) produced by Microcystis aeruginosa when exposed to linoleic acid (LA) and LA sustained-release microspheres, categorizing them into soluble, loosely bound, and tightly bound EPS.
  • - The study utilized 3D-EEM fluorescence spectroscopy and FTIR spectrometry to assess the composition of these EPS types, finding specific proteins and polysaccharides across all fractions, with tryptophan and humic acid-like substances present in varying amounts.
  • - Results indicated the highest inhibitor rate occurred at a concentration of 0.3 g/L of LA, and while the functional groups in the EPS did not change significantly, distinct differences in aromatic proteins were noted

Article Abstract

This paper focuses on the characterization of extracellular polymeric substances (EPS), which are composed of soluble EPS (SL-EPS), loosely bound EPS (LB-EPS), and tightly bound EPS (TB-EPS) produced by Microcystis aeruginosa under the stress of linoleic acid (LA) and LA sustained-release microspheres. Three-dimensional excitation-emission matrix (3D-EEM) fluorescence spectroscopy and Fourier transform infrared (FTIR) spectrometry were used to characterize three forms of EPS while the content of polysaccharide and protein was tested, respectively. The results showed that the highest inhibitor rate (IR) occurred when M. aeruginosa were exposed to LA sustained-release microspheres of 0.3 g L. The 3D-EEM contour demonstrated that tryptophan and protein-like substances were detected in all three EPS fractions, whereas humic acid-like substance was only distributed in SL-EPS, and aromatic proteins merely existed in LB-EPS and TB-EPS. The infrared spectrum showed that functional groups in three EPS fractions had no obvious change in all experimental groups. Polysaccharide (1120-1270 cm, C-O-C and C-O stretching vibration) and protein (1384-1670 cm, C-N and N-H stretching) were detected in three forms of EPS. Graphical abstract ᅟ.

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Source
http://dx.doi.org/10.1007/s11356-017-9540-1DOI Listing

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