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opencc-by-4.0Mar 2023View details →

Test of cultivation of different macroalgae species and structures in shrimp ponds

<table> <tbody> <tr> <td> <p><strong>Shrimp monoculture suffers drastic productivity reduction due to the white spot syndrome outbreak. Integrated multitrophic aquaculture (IMTA) is an alternative to alleviate this problem. Farming autotrophic and filter-feeding organisms with shrimps results in bioremediation of the system, production diversification, and extra income for farmers. We performed a factorial-designed experiment in a commercial shrimp farm, Primar Aquaculture - RN. We tested different species and farming structures of macroalgae for cultivation with shrimps in ponds. The tested macroalgae species were from genera Ulva, Gracilaria, and Hypnea. The structures tested were tubular nets, trays, pillows, and long lines. Macroalgae farming lasted 59 days. We monitored the water parameters temperature, dissolved oxygen, pH, and salinity. All the treatments presented macroalgae biomass loss. The results indicate no technical feasibility of farming the tested macroalgae species in the shrimp's earthen ponds. </strong></p> </td> </tr> </tbody> </table>

opencc-by-4.0Mar 2023View details →

Data for Macroalgae exhibit diverse responses to human disturbances on coral reefs

<p>Percent cover of macroalgae data used in the analyses described in the Global Change Biology publication, <em>Macroalgae exhibit diverse responses to human disturbances on coral reefs (</em>DOI: 10.1111/GCB.16694)</p>

Fig. 5 in Polyketide-derived macrobrevins from marine macroalga-associated Bacillus amyloliquefaciens as promising antibacterial agents against pathogens causing nosocomial infections

Fig. 5. (A) Molecular docking interfaces of 41-hydroxy-macrobrevin-31-acetate (compound 3) with S. aureus peptide deformylase (SaPDF). 3D docking analysis of the titled macrobrevin analogue (ligand) and S. aureus PDF crystal structure (PDB ID: 1LQW) were conformationally structured (Swiss-Pdb Viewer, SPDBV, version 4.1.0). The primary algorithm used by AutoDock for conformational searching was the Lamarckian Genetic Algorithm (LGA) showing four hydrogen bonds each (displayed as red and bluecoloured lines) in the binding site, whereas USCF Chimera (University of California, San Francisco, ver. 1.11.2) software reinforced the visualizations of the best molecular docking positions of the compound and target protein. The contact residues were shown and labeled by type and number in the background. Compound 3 exhibited least binding energy among the titled compounds. (B) Illustrative representation of 41-hydroxy-macrobrevin-31-acetate (compound 3) forming hydrogen bond interactions with the amino acyl residues in the active site of SaPDF. Compound (3) displayed maximum number of hydrogen bond interactions (GLN141 at 3.118 Å, LYS84 at 3.789 Å and 3.388 Å, and ARG143 at 3.483 Å). (C) Drug-likeness score obtained for the compound (3) with molsoft software. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 4 in Polyketide-derived macrobrevins from marine macroalga-associated Bacillus amyloliquefaciens as promising antibacterial agents against pathogens causing nosocomial infections

Fig. 4. Proposed biosynthesis of 21- membered macrocyclic lactones classified as macrobrevin analogues (1–4) in B. amyloliquefaciens through successive decarboxylative Claisen condensation between acetyl-S-KS domain and malonate-SACP units. Claisen condensation was activated by acyl carrier protein (ACP), ketoreductase (KR), ketosynthase (KS), thioesterase (TE), dehydratase (DH), methyl transferase (MT), acyl transferase (AT), enoyl reductase (ER) and S-adenosyl-methionine (SAM). The elongation process comprised of 16 modules with KS, KR and ACP domains. The initial step includes the decarboxylative Claisen condensation between 2-methylbutanethioic-S-KS and malonate-S-ACP. The final step of macrobrevin formation could occur through the cyclization of linear chain of 21-membered carbon framework by TE. Consequently, alterations of 21-membered carbon framework classified as macrobrevin scaffold could result in the formation of macrobrevin analogues 1–4.

Fig. 3 in Polyketide-derived macrobrevins from marine macroalga-associated Bacillus amyloliquefaciens as promising antibacterial agents against pathogens causing nosocomial infections

Fig. 3. (A) Biosynthetic gene cluster coding for biosynthesis of macrobrevin analogues in B. amyloliquefaciens showing 46% similarity with macrobrevin biosynthetic gene cluster BGC0001470 (as elucidated by Known-Cluster-Blast prediction, the gene cluster also had 32% similarity with aurantinine and bacillaene with 100% similarity), (B) organization of genes in macrobrevin biosynthetic gene cluster of Brevibacillus sp. (C) Domain organization of the modules of trans-AT PKS gene cluster coding for bacillaene, which is 46% similar to macrobrevin biosynthetic gene cluster is shown. (D) The proposed functions of genes (1–16) contained in the biosynthetic gene cluster has been listed out, and are described as: (1) Biosynthetic additional (smcogs) SMCOG1170: metallo-β-lactamase family protein (score: 203; E-value: 5.4e-62); (2) biosynthetic trans-AT-PKS:PKS_AT biosynthetic additional SMCOG1021: malonyl CoA-acyl carrier protein transacylase (score: 400.8; E-value: 1.8e-121); (3) biosynthetic trans AT-PKS:PKS_AT biosynthetic additional SMCOG1021: malonyl CoA-acyl carrier protein transacylase (score: 232.8; E-value: 1.5e-70); (4) biosynthetic trans-AT-PKS:PKS_AT biosynthetic additional SMCOG1021:malonyl CoA-acyl carrier protein transacylase (score: 481.1; E-value: 9e-146); (5) biosynthetic additional PP-binding; (6) biosynthetic T3PKS:Chal_sti_synt_N biosynthetic additional SMCOG1043:hydroxymethylglutaryl-CoA synthase (score: 496.9; E-value: 6.5e-151); (7) biosynthetic additional SMCOG1023: enoyl-CoA hydratase (score: 228.4; E-value: 1.3e-69); (8) biosynthetic trans-AT-PKS:PP-binding biosynthetic trans-AT-PKS:tra_KS-biosynthetic trans AT-PKS:ATd-biosynthetic NRPS:AMP-binding biosynthetic-NRPS: condensation biosynthetic additional adh_short biosynthetic additional SMCOG1127: condensation domain-containing protein (score: 295.3; E-value: 1.6e-89); (9) biosynthetic additional-tra_KS biosyntheticadditional SMCOG1022: β-ketoacyl synthase (score: 160.9; E-value: 8.3e-49); (10) biosynthetic-trans-AT-PKS:PP-binding-biosynthetic-trans-AT-PKS:tra_KS-biosynthetic-trans-AT-KS:ATd-biosynthetic-additional-adh_short-biosynthetic-additional-SMCOG1001:short-chain-dehydrogenase/reductase SDR (score: 48.7; E-value: 1.2e-14); (11) biosynthetic-trans-AT-PKS:PP-binding-biosynthetic-trans-AT-PKS:tra_KS-biosynthetic-trans-AT-PKS:ATd-biosynthetic-additional-adh_short-biosynthetic-additional SMCOG1093: β-ketoacyl synthase (score: 73.2; E-value: 2.8e-22); (12) biosynthetic trans AT-PKS: PP-binding-biosynthetic-trans-AT-PKS:tra_KSbiosynthetic-trans-AT-PKS:ATd-biosynthetic-additional-adh biosynthetic-additional SMCOG1022: β-ketoacyl synthase (score: 222.6; E-value: 1.5e-67); (13) biosynthetic-additional-condensation biosynthetic-additional SMCOG1127:condensation domain-containing protein (score: 196.8; E-value: 1.3e-59); (14) biosynthetic-trans-AT-PKS:PP-binding-biosynthetic-trans-AT-PKS:tra_KS-biosynthetic-trans-AT-PKS:ATd-biosynthetic-NRPS-like:AMP-binding-biosynthetic-NRPS-like:PPbinding-biosynthetic-additional adh_short-biosynthetic-additional SMCOG1002: AMP-dependent synthetase and ligase (score: 373.7; E-value: 1.9e-113); (15) biosynthetic-additional-PP-binding-biosynthetic-additional-tra_KS-biosynthetic-additional MCOG1022: β-ketoacyl (score: 73.2; E-value: 2.8e-22); (16) biosynthetictrans-AT-PKS-like:tra_KS-biosynthetic-trans-AT-PKS-like:ATd-biosynthetic-additional-PP-binding-biosynthetic-additional SMCOG1022: β-ketoacyl synthase (score: 207.7; E-value: 5.1e-63).

Fig. 1 in Polyketide-derived macrobrevins from marine macroalga-associated Bacillus amyloliquefaciens as promising antibacterial agents against pathogens causing nosocomial infections

Fig. 1. Structural representation of (A) trihydroxy-decahydro-37-methyl-macrobrevin (compound 1), (B) hexahydro-macrobrevin (compound 2), (C) hexahydro-41- hydroxy-macrobrevin-31-acetate (compound 3), and (D) hexahydro-28-nor-methyl-5-methoxy-macrobrevin (compound 4) isolated from marine macroalgaassociated B. amyloliquefaciens MTCC 12713. (E) The zone of inhibition (34 mm) observed with hexahydro-41-hydroxy-macrobrevin-31-acetate (compound 3) against VREfs as visualized on Mueller Hinton agar plates by disc diffusion assay was illustrated. The amounts of compound 3 and chloramphenicol were 30 μg per disc. Chloramphenicol and ethyl acetate, which were used as the positive and negative control, were denoted with (+) and (), respectively.

Fig. 2. 1H–1H in Polyketide-derived macrobrevins from marine macroalga-associated Bacillus amyloliquefaciens as promising antibacterial agents against pathogens causing nosocomial infections

Fig. 2. 1H–1H COSY/HMBC (A-D) correlations of macrobrevin analogues (1–4). Key 1H–1H COSY correlations and HMBC pairings were characterized by bold-faced bonds and double-barbed arrows, respectively.

Fig. 4 in Survey of the allelopathic potential of Mediterranean macroalgae: production of long-chain polyunsaturated aldehydes (PUAs)

Fig. 4. Relative abundance (%) of aldehydes in macroalgae sampled in July 2017 (A) and April 2018 (B).

Fig. 3 in Survey of the allelopathic potential of Mediterranean macroalgae: production of long-chain polyunsaturated aldehydes (PUAs)

Fig. 3. Representative chromatograms (m/z 181) of standard compounds and algal extracts: (A) standards; (B) Ulva cf. rigida; (C) Dictyopteris polypodioides. The numbers 1–13 correspond to the oxime derivates of the putatively identified substances: (1) hexadienal; (2) benzaldehyde; (3) 2,4-heptadienal; (4) 2,4- octadienal; (5) 2,4-decadienal; (6) nonatetraenal; (7) nonatrienal; (8) decatetraenal; (9) hexadecadienal; (10) pentadecanal/hexadecaheptaenal; (11) tetradecapentaenal; (12) hexadecatrienal; (13) hexadecatetraenal.

Fig. 2 in Survey of the allelopathic potential of Mediterranean macroalgae: production of long-chain polyunsaturated aldehydes (PUAs)

Fig. 2. Total aldehydes production (nmol g 1) in Mediterranean macroalgae (data are mean ± st. dev. of 3 replicates).

Fig. 5 in Survey of the allelopathic potential of Mediterranean macroalgae: production of long-chain polyunsaturated aldehydes (PUAs)

Fig. 5. Aldehydes production (nmol g 1) by Dictyopteris polypodioides at the different sampling times (data are mean ± st. dev. of 3 replicates).

Fig. 7. A in Survey of the allelopathic potential of Mediterranean macroalgae: production of long-chain polyunsaturated aldehydes (PUAs)

Fig. 7. A: Map indicating the position of the sampling site (Piscinetta del Passetto). B, C: details of the phytobenthic community in July 2017. In Fig. 6B arrowhead indicates Cystoseira compressa, curved arrow Dictyopteris polypodioides, and straight arrow Ulva cf. rigida, three of the species used for extraction of PUAs.

Fig. 6 in Survey of the allelopathic potential of Mediterranean macroalgae: production of long-chain polyunsaturated aldehydes (PUAs)

Fig. 6. Aldehydes production (nmol g 1) by Ulva cf. rigida at the different sampling times (data are mean ± st. dev. of 3 replicates).

Fig. 2 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties

Fig. 2. (A1-C1) 1H–1H COSY (bold-face bonds), selected HMBCs (double-barbed arrows), (A2-C2) NOE (colored arrows) correlations of conoidecyclics A-C isolated from T. conoides and (A3-C3) computer-generated models using MM2 force field calculations were displayed.

Fig. 5 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties

Fig. 5. (A1-A2) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of COX-2; (A3-A4) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of 5-LOX; (A5-A6) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of PTP-1B; (A7-A8) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of ACE as obtained from in silico molecular docking analysis.

Fig. 3 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties

Fig. 3. (A1-A2) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of COX-2; (A3-A4) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of 5-LOX; (A5-A6) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of PTP-1B; (A7-A8) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of ACE as obtained from in silico molecular docking analysis.

Fig. 1 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties

Fig. 1. Structural representations of conoidecyclics A-C purified from the solvent extract of T. conoides. The thallus structure (leaf-like) of T. conoides was illustrated.

Fig. 4 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties

Fig. 4. (A1-A2) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of COX-2; (A3-A4) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of 5-LOX; (A5-A6) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of PTP-1B; (A7-A8) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of ACE as obtained from in silico molecular docking analysis.

Fig. 6 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties

Fig. 6. Kinetic studies of the pharmacologic response with regard to inhibition mode of ACE-I (A–C), PTP-1B (D–F) and 5-LOX (G–I), respectively to the studied conoidecyclics A-C. Representation of Dixon plots for conoidecyclics A-C, for the determination of the inhibition constant Ki. The Ki value was determined from the negative X-axis value at the point of the intersection of the four lines. The data were expressed as the mean reciprocal of initial velocity for triplicates (n = 3) at each substrate concentration. Different concentrations of isolated compounds were used, and the inhibitory potentials were expressed in mM.