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Data Phytochemical, antioxidant, antimicrobial, and protein binding qualities of hydro-ethanolic extract of Tinospora cordifolia S1. Qualitative analysis of phytochemicalsSmall branches and stem bark extracts (petroleum ether, acetone and methanol) of TC were analyzed for the presence of various phytochemicals using the respective chemical tests as follows. S1.1. Test for glycosides0.5 mL extract was taken in a test tube, 0.2 mL of 10 % ferric chloride solution and (50 %) glacial acetic acid added. Few drops of concentrated sulphuric acid were added. A blue color production shows the presence of glycosides. S1.2. Tests for terpenoidsExtract was mixed with chloroform and a few drops of conc. H 2 SO 4 were added, shaken well and allowed to stand for some time. Red color appeared at the lower layer indicated the presence of steroids and formation of yellow colored layer indicated the presence of terpenoids. S1.3. Test for proteinsAn aliquot of 2 mL of extract was treated with one drop of 2% copper sulphate solution. To this, 1 mL of ethanol (90%) was added, followed by excess of potassium hydroxide pellets. Pink color in ethanol layer indicated the presence of proteins. S1.4. Test for amino acidsTwo drops of ninhydrine (5%) were added to 1 mL of extract. A characteristic purple color indicated the presence of amino acids. S1.5. Test for alkaloidsTwo millilitre of 1 % HCl was mixed with 0.1 gm of crude extract and heated slightly. After cooling Wagner's reagent and Mayer's reagent were added to it. The presence of buff colored precipitate indicated the presence of alkaloids. S1.6. Test for carbohydratesBenedict's reagents was mixed with the 1 mL of crude extract and slightly boiled, appearance of reddish brown precipitate indicated the presence of the carbohydrates. S1.7. Test for flavonoidsThe appearance of pink scarlet color when 1 mL of crude extract was mixed with few drops of concentrated HCl and Mg pellets indicated the presence of flavonoids. S1.8. Test for phenols2 mL of 2 % ferric chloride was mixed with the 1 mL of crude extract and the presence of bluegreen or black coloration indicated the presence of phenols.

This review provides an insight into the regulation of the carbon concentrating mechanisms (CCMs) in lower organisms like cyanobacteria, proteobacteria, and algae. CCMs evolved as a mechanism to concentrate CO at the site of primary carboxylating enzyme Ribulose-1, 5-bisphosphate carboxylase oxygenase (Rubisco), so that the enzyme could overcome its affinity towards O which leads to wasteful processes like photorespiration. A diverse set of CCMs exist in nature, i.e., carboxysomes in cyanobacteria and proteobacteria; pyrenoids in algae and diatoms, the C system, and Crassulacean acid metabolism in higher plants. Prime regulators of CCM in most of the photosynthetic autotrophs belong to the LysR family of transcriptional regulators, which regulate the activity of the components of CCM depending upon the ambient CO concentrations. Major targets of these regulators are carbonic anhydrase and inorganic carbon uptake systems (CO and HCO transporters) whose activities are modulated either at transcriptional level or by changes in the levels of their co-regulatory metabolites. The article provides information on the localization of the CCM components as well as their function and participation in the development of an efficient CCM. Signal transduction cascades leading to activation/inactivation of inducible CCM components on perception of low/high CO stimuli have also been brought into picture. A detailed study of the regulatory components can aid in identifying the unraveled aspects of these mechanisms and hence provide information on key molecules that need to be explored to further provide a clear understanding of the mechanism under study.

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