Can Microcystis spp. blooms be used in animal feeds?

A recent paper by Chen et al. published in Science of the Total Environment reviews the challenges of using blooms of Microcystis spp. in animal feeds.

Highlights (from the paper):

  • Microcystis causes toxicity to mollusks, crustaceans, fish, amphibians, mammals and birds.
  • Microcystis induces toxicity in liver, kidney, intestine, spleen and other organs.
  • Fish fed Microcystis may be not safe for consumption for humans.
  • Microbial pathogens may be present in cyanobacterial blooms.

Reference:

Liang Chen, John P. Giesy, Ondrej Adamovsky, Zorica Svirčev, Jussi Meriluoto, Geoffrey A. Codd, Biljana Mijovic, Ting Shi, Xun Tuo, Shang-Chun Li, Bao-Zhu Pan, Jun Chen, Ping Xie.
Challenges of using blooms of Microcystis spp. in animal feeds: A comprehensive review of nutritional, toxicological and microbial health evaluation. Science of The Total Environment, Volume 764, 2021, https://doi.org/10.1016/j.scitotenv.2020.142319

Microginins from a Microcystis sp. Bloom Material Collected from the Kishon Reservoir, Israel

From the abstract of a recent paper by Anat Lodin-Friedman and Shmuel Carmeli, published in Marine Drugs:

“During blooms, cyanobacteria produce diverse modified peptides. Among these are the microginins, which inhibit zinc-containing metalloproteases. Ten microginins, microginins KR767 (1), KR801(2), KR835 (3), KR785 (4), KR604 (5), KR638 (6), KR781 (7), KR815 (8), FR3 (9), and FR4 (10), were isolated from the extract of a bloom material of Microcystis sp. (IL-405) collected from the Kishon Reservoir, Israel in the fall of 2009. The structures of the pure compounds were elucidated using 1D and 2D NMR techniques and high-resolution mass spectrometry. The absolute configuration of the chiral centers of the amino acids were determined by Marfey’s and advance Marfey’s methods and by comparison of 1H and 13C NMR chemical shifts of the Ahda derivatives with those of known microginins. These microginins differ in sequence and absolute configuration of the chiral centers of the Ahda moieties and by N-methylation of the Ahda amine group and extent of chlorination of the Ahda terminal methyl group. The compounds were evaluated for inhibition of the zinc metalloprotease, aminopeptidase M, and exhibited low- to sub-nanomolar half maximal inhibitory concentration (IC50) values”.

Reference:

Lodin-Friedman, A.; Carmeli, S. Microginins from a Microcystis sp. Bloom Material Collected from the Kishon Reservoir, Israel. Mar. Drugs 2018, 16, 78. https://doi.org/10.3390/md16030078