Green Synthesis of Zinc Oxide (ZnO) Nanoparticles from Green Algae and Their Assessment in Various Biological Applications.

The biosynthesis of algal-based zinc oxide (ZnO) nanoparticles has shown several advantages over traditional physico-chemical methods, such as lower cost, less toxicity, and greater sustainability. In the current study, bioactive molecules present in Spirogyra hyalina extract were exploited for the biofabrication and capping of ZnO NPs, using zinc acetate dihydrate and zinc nitrate hexahydrate as precursors. The newly biosynthesized ZnO NPs were characterized for structural and optical changes through UV-Vis spectroscopy, Fourier transform infrared spectroscopy (FT-IR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and energy dispersive X-ray spectroscopy (EDX). A color change in the reaction mixture from light yellow to white indicated the successful biofabrication of ZnO NPs. The UV-Vis absorption spectrum peaks at 358 nm (from zinc acetate) and 363 nm (from zinc nitrate) of ZnO NPs confirmed that optical changes were caused by a blue shift near the band edges. The extremely crystalline and hexagonal Wurtzite structure of ZnO NPs was confirmed by XRD. The involvement of bioactive metabolites from algae in the bioreduction and capping of NPs was demonstrated by FTIR investigation. The SEM results revealed spherical-shaped ZnO NPs. In addition to this, the antibacterial and antioxidant activity of the ZnO NPs was investigated. ZnO NPs showed remarkable antibacterial efficacy against both Gram-positive and Gram-negative bacteria. The DPPH test revealed the strong antioxidant activity of ZnO NPs.

Biosorption of Cadmium and Lead by Dry Biomass of Nostoc sp. MK-11: Kinetic and Isotherm Study.

Cadmium (Cd) and lead (Pb) are global environmental pollutants. In this study, Nostoc sp. MK-11 was used as an environmentally safe, economical, and efficient biosorbent for the removal of Cd and Pb ions from synthetic aqueous solutions. Nostoc sp. MK-11 was identified on a morphological and molecular basis using light microscopic, 16S rRNA sequences and phylogenetic analysis. Batch experiments were performed to determine the most significant factors for the removal of Cd and Pb ions from the synthetic aqueous solutions using dry Nostoc sp. MK1 biomass. The results indicated that the maximum biosorption of Pb and Cd ions was found under the conditions of 1 g of dry Nostoc sp. MK-11 biomass, 100 mg/L of initial metal concentrations, and 60 min contact time at pH 4 and 5 for Pb and Cd, respectively. Dry Nostoc sp. MK-11 biomass samples before and after biosorption were characterized using FTIR and SEM. A kinetic study showed that a pseudo second order kinetic model was well fitted rather than the pseudo first order. Three isotherm models Freundlich, Langmuir, and Temkin were used to explain the biosorption isotherms of metal ions by Nostoc sp. MK-11 dry biomass. Langmuir isotherm, which explains the existence of monolayer adsorption, fitted well to the biosorption process. Considering the Langmuir isotherm model, the maximum biosorption capacity (qmax) of Nostoc sp. MK-11 dry biomass was calculated as 75.757 and 83.963 mg g-1 for Cd and Pb, respectively, which showed agreement with the obtained experimental values. Desorption investigations were carried out to evaluate the reusability of the biomass and the recovery of the metal ions. It was found that the desorption of Cd and Pb was above 90%. The dry biomass of Nostoc sp. MK-11 was proven to be efficient and cost-effective for removing Cd and especially Pb metal ions from the aqueous solutions, and the process is eco-friendly, feasible, and reliable.

Growth Optimization and Secondary Metabolites Evaluation of Anabaena variabilis for Acetylcholinesterase Inhibition Activity.

Cyanobacteria comprise a good natural resource of a potential variety of neuro-chemicals, including acetylcholinesterase inhibitors essential for Alzheimer's disease treatment. Accordingly, eight different cyanobacterial species were isolated, identified, and evaluated on their growth on different standard nutrient media. It was found that the modified Navicula medium supported the highest growth of the test cyanobacteria. The effects of methylene chloride/methanol crude extracts of the test cyanobacteria on acetylcholinesterase activity were examined and compared. Anabaena variabilis (KU696637.1) crude extract recorded the highest acetylcholinesterase inhibition (62 ± 1.3%). Navicula medium chemical components were optimized through a Plackett-Burman factorial design. The biomass of Anabaena variabilis increased significantly when grown on the optimized medium compared to that of control. The chemical analysis of the fractions derived from Anabaena variabilis showed the presence of two compounds in significant amounts: the flavonoid 5,7-dihydroxy-2-phenyl-4H-chrome-4-one and the alkaloid 4-phenyl-2-(pyridin-3-yl) quinazoline. Molecular docking studies revealed that both compounds interact with the allosteric binding site of acetylcholinesterase at the periphery with π-π stackings with Tyr341 and Trp286 with good, predicted partition coefficient. The compounds obtained from this study open the door for promising drug candidates to treat Alzheimer's disease for their better pharmacodynamics and pharmacokinetic properties.

CpeY is a phycoerythrobilin lyase for cysteine 82 of the phycoerythrin I α-subunit in marine Synechococcus.

Marine Synechococcus are widespread in part because they are efficient at harvesting available light using their complex antenna, or phycobilisome, composed of multiple phycobiliproteins and bilin chromophores. Over 40% of Synechococcus strains are predicted to perform a type of chromatic acclimation that alters the ratio of two chromophores, green-light-absorbing phycoerythrobilin and blue-light-absorbing phycourobilin, to optimize light capture by phycoerythrin in the phycobilisome. Lyases are enzymes which catalyze the addition of bilin chromophores to specific cysteine residues on phycobiliproteins and are involved in chromatic acclimation. CpeY, a candidate lyase in the model strain Synechococcus sp. RS9916, added phycoerythrobilin to cysteine 82 of only the α subunit of phycoerythrin I (CpeA) in the presence or absence of the chaperone-like protein CpeZ in a recombinant protein expression system. These studies demonstrated that recombinant CpeY attaches phycoerythrobilin to as much as 72% of CpeA, making it one of the most efficient phycoerythrin lyases characterized to date. Phycobilisomes from a cpeY- mutant showed a near native bilin composition in all light conditions except for a slight replacement of phycoerythrobilin by phycourobilin at CpeA cysteine 82. This demonstrates that CpeY is not involved in any chromatic acclimation-driven chromophore changes and suggests that the chromophore attached at cysteine 82 of CpeA in the cpeY- mutant is ligated by an alternative phycoerythrobilin lyase. Although loss of CpeY does not greatly inhibit native phycobilisome assembly in vivo, the highly active recombinant CpeY can be used to generate large amounts of fluorescent CpeA for biotechnological uses.

Adaptation to Blue Light in Marine Synechococcus Requires MpeU, an Enzyme with Similarity to Phycoerythrobilin Lyase Isomerases.

Marine Synechococcus has successfully adapted to environments with different light colors, which likely contributes to this genus being the second most abundant group of microorganisms worldwide. Populations of Synechococcus that grow in deep, blue ocean waters contain large amounts of the blue-light absorbing chromophore phycourobilin (PUB) in their light harvesting complexes (phycobilisomes). Here, we show that all Synechococcus strains adapted to blue light possess a gene called mpeU. MpeU is structurally similar to phycobilin lyases, enzymes that ligate chromophores to phycobiliproteins. Interruption of mpeU caused a reduction in PUB content, impaired phycobilisome assembly and reduced growth rate more strongly in blue than green light. When mpeU was reintroduced in the mpeU mutant background, the mpeU-less phenotype was complemented in terms of PUB content and phycobilisome content. Fluorescence spectra of mpeU mutant cells and purified phycobilisomes revealed red-shifted phycoerythrin emission peaks, likely indicating a defect in chromophore ligation to phycoerythrin-I (PE-I) or phycoerythrin-II (PE-II). Our results suggest that MpeU is a lyase-isomerase that attaches a phycoerythrobilin to a PEI or PEII subunit and isomerizes it to PUB. MpeU is therefore an important determinant in adaptation of Synechococcus spp. to capture photons in blue light environments throughout the world's oceans.