Review of Marine Cyanobacteria and the Aspects Related to Their Roles: Chemical, Biological Properties, Nitrogen Fixation and Climate Change.

Marine cyanobacteria are an ancient group of photosynthetic microbes dating back to 3.5 million years ago. They are prolific producers of bioactive secondary metabolites. Over millions of years, natural selection has optimized their metabolites to possess activities impacting various biological targets. This paper discusses the historical and existential records of cyanobacteria, and their role in understanding the evolution of marine cyanobacteria through the ages. Recent advancements have focused on isolating and screening bioactive compounds and their respective medicinal properties, and we also discuss chemical property space and clinical trials, where compounds with potential pharmacological effects, such as cytotoxicity, anticancer, and antiparasitic properties, are highlighted. The data have shown that about 43% of the compounds investigated have cytotoxic effects, and around 8% have anti-trypanosome activity. We discussed the role of different marine cyanobacteria groups in fixing nitrogen percentages on Earth and their outcomes in fish productivity by entering food webs and enhancing productivity in different agricultural and ecological fields. The role of marine cyanobacteria in the carbon cycle and their outcomes in improving the efficiency of photosynthetic CO2 fixation in the chloroplasts of crop plants, thus enhancing the crop plant's yield, was highlighted. Ultimately, climate changes have a significant impact on marine cyanobacteria where the temperature rises, and CO2 improves the cyanobacterial nitrogen fixation.

Heterologous expression of the antifungal ß-chitin binding protein CBP24 from bacillus thuringiensis and its synergistic action with bacterial chitinases.

The genome sequence analysis of Bacillus thuringiensis serovar konkukian S4 has shown to contain two chitinases (Chi74, Chi39) and two chitin-binding proteins (CBP50 and CBP24). The Chi74, Chi39 and CBP50 have been characterized previously. The chitin-binding protein CBP24 was cloned and heterologously expressed in Escherichia coli. The recombinant protein was purified using a Ni-NTA purification system. The purified protein was used to study its substrate binding activity using crystalline chitin variants as substrates. The Bmax and Kd values have shown that it preferably binds to ß-type of the crystalline chitin at a range of pH with peak activity between 5.5-7.5. To elucidate the role of CBP24 in the chitin degradation system of S4, the purified chitinases Chi74, Chi39 along with the ChiA from Serratia proteamcualans were used in different combinations with the CBP24 and chitinolytic activity was assayed. It was shown that the CBP24 acts synergistically with chitin degradation activity of bacterial chitinases non-specifically. Moreover, the CBP24 has shown antifungal activity against plant pathogenic fungi Fusarium oxysporum and Rhizoctonia solani. The present study will lead us to develop a technology for environmental friendly conversion of chitin to valuable products.

Thermodynamic properties of the ß-glucosidase from Thermotoga maritima extend the upper limit of thermophilicity.

Enzymes from thermophilic organisms are believed to be strong candidates for industrial applications due to their ability to withstand temperature-induced enzyme inactivation. The present study demonstrated molecular cloning, over-expression, purification and characterization of ß-glucosidase from Thermotoga maritima. The bglA gene with a capacity to encode a 51 kDa enzyme was heterologously expressed in E. coli M15. The enzyme was produced @130 mgL(-1) in LB media and @440 mgL(-1) in Dubos salt medium accounting 40-47 % of total cellular soluble proteins when lactose was used as an inducer. The enzyme showed a peak activity between pH and temperature range of 5.0-7.0 and 80-100 °C, respectively. The activity was fairly stable up to 140 °C. The turnover rate (kcat) of the enzyme was 187.1±20 s(-1), whereas the Km and Vmax values were 0.56 mM and 238±2.4 IU mg(-1) protein, respectively. The enzyme was shown to have half-life of 136, 71 and 12.6 h at 80, 90 and 100 °C, respectively. Thermodynamics parameters including melting temperature (130 °C), activation energy for inactivation (36.92 kJmole(-1)), enthalpy (33.73 kJmole(-1)), Gibb's free energy (127.96 kJmole(-1)) and entropy (-246.46 Jmole(-1)K(-1)) have shown that the enzyme have enhanced hydrophobic interactions to prevent its thermal unfolding. These features endorse the industrial applications of the enzyme.