Abstract

Microalgae and cyanobacteria are good sources for prospecting metabolites of biotechnological interest, including glucosidase inhibitors. These inhibitors act on enzymes related to various biochemical processes; they are involved in metabolic diseases, such as diabetes and Gaucher disease, tumors and viral infections, thus, they are interesting hubs for the development of new drugs and therapies. In this work, the screening of 63 environmental samples collected in the Brazilian Amazon found activity against β-glucosidase, of at least 60 min, in 13.85% of the tested extracts, with Synechococcus sp. GFB01 showing inhibitory activity of 90.2% for α-glucosidase and 96.9% against β-glucosidase. It was found that the nutritional limitation due to a reduction in the concentration of sodium nitrate, despite not being sufficient to cause changes in cell growth and photosynthetic apparatus, resulted in reduced production of α and β-glucosidase inhibitors and differential protein expression. The proteomic analysis of cyanobacteria isolated from the Amazon is unprecedented, with this being the first work to evaluate the protein expression of Synechococcus sp. GFB01 subjected to nutritional stress. This evaluation helps to better understand the metabolic responses of this organism, especially related to the production of inhibitors, adding knowledge to the industrial potential of these cyanobacterial compounds.

Highlights

  • IntroductionGlucosidases are important enzymes for the correct functioning of various physiological systems, as they are involved in biochemical processes such as the degradation of polysaccharides to monosaccharides—the latter being the form absorbable by our body

  • We evaluated the differential proteome of the α and β-glucosidase inhibitor-producing strain, Synechococcus sp

  • The literature places nitrogen as most significant for β-glucosidase inhibition [11], the results show that the production of α-glucosidase inhibitors was more affected by nutritional stress

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Summary

Introduction

Glucosidases are important enzymes for the correct functioning of various physiological systems, as they are involved in biochemical processes such as the degradation of polysaccharides to monosaccharides—the latter being the form absorbable by our body. —and they are responsible for the intracellular digestion of lysosomal glycoconjugates and glycoprotein as well as glycolipid biosynthesis from oligosaccharides [1,2]. Glycoconjugates are present on the surface of cells, acting on cell recognition and playing an important role in viral and bacterial infections, in addition to other immune responses; the Microorganisms 2021, 9, 1593. Microorganisms 2021, 9, 1593 malfunction of glycoconjugate synthesis can result in immature glycoproteins, which can affect the solubility of molecules, cause inflammatory processes, and develop tumor cells [3,4,5,6]. The inhibitors act in a competitive manner, preventing the action of these enzymes and avoiding postprandial hyperglycemia [7,8,9]

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