Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin Glycosides
This study was designed to investigate the structure of synthesized hesperidin glycosides (HGs) and evaluate their antibacterial and α-glucosidase inhibitory activities. The preliminary structure of HG<sub>s</sub> was confirmed by glucoamylase treatment and analyzed on thin layer chromat...
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MDPI AG
2021-04-01
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| Online Access: | https://www.mdpi.com/2073-4344/11/5/532 |
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| author | Titaporn Chaisin Prakarn Rudeekulthamrong Jarunee Kaulpiboon |
| author_facet | Titaporn Chaisin Prakarn Rudeekulthamrong Jarunee Kaulpiboon |
| author_sort | Titaporn Chaisin |
| collection | DOAJ |
| description | This study was designed to investigate the structure of synthesized hesperidin glycosides (HGs) and evaluate their antibacterial and α-glucosidase inhibitory activities. The preliminary structure of HG<sub>s</sub> was confirmed by glucoamylase treatment and analyzed on thin layer chromatography (TLC). The LC-MS/MS profiles of HGs showed the important fragments at m/z ratios of 345.21 (added glucose to glucose of rutinose in HG<sub>1</sub>) and 687.28 (added maltose to glucose of rutinose in HG<sub>2</sub>), confirming that the structures of HG<sub>1</sub> and HG<sub>2</sub> were α-glucosyl hesperidin and α-maltosyl hesperidin, respectively. In addition, <sup>1</sup>H and <sup>13</sup>C-NMR of hesperidin derivatives were performed to identify their α-1,4-glycosidic bonds. The MIC and MBC studies showed that transglycosylated HG<sub>1</sub> and HG<sub>2</sub> had better antibacterial and bactericidal activities than hesperidin and diosmin, and were more active against <i>Staphylococcus aureus</i> than <i>Escherichia coli</i>. Hesperidin, HG<sub>1</sub>, HG<sub>2</sub>, and diosmin inhibited α-glucosidase with IC<sub>50</sub> values of 2.75 ± 1.57, 2.48 ± 1.61, 2.36 ± 1.48, and 2.99 ± 1.23 mg/mL, respectively. The inhibition kinetics of HG<sub>2</sub> shown by a Lineweaver–Burk plot confirmed HG<sub>2</sub> was an α-glucosidase competitive inhibitor with an inhibitor constant, <i>K</i><sub>i</sub>, of 2.20 ± 0.10 mM. Thus, HGs have the potential to be developed into antibacterial drugs and treatments for treating α-glucosidase-associated type 2 diabetes. |
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| language | English |
| last_indexed | 2024-03-10T12:07:04Z |
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| spelling | doaj.art-cfbdf8a58bda4410be93c851887d9aa12023-11-21T16:32:53ZengMDPI AGCatalysts2073-43442021-04-0111553210.3390/catal11050532Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin GlycosidesTitaporn Chaisin0Prakarn Rudeekulthamrong1Jarunee Kaulpiboon2Protein Research Laboratory, Division of Biochemistry, Department of Pre-Clinical Science, Faculty of Medicine, Thammasat University, Pathumthani 12120, ThailandDepartment of Biochemistry, Phramongkutklao College of Medicine, Phramongkutklao Hospital, Bangkok 10400, ThailandProtein Research Laboratory, Division of Biochemistry, Department of Pre-Clinical Science, Faculty of Medicine, Thammasat University, Pathumthani 12120, ThailandThis study was designed to investigate the structure of synthesized hesperidin glycosides (HGs) and evaluate their antibacterial and α-glucosidase inhibitory activities. The preliminary structure of HG<sub>s</sub> was confirmed by glucoamylase treatment and analyzed on thin layer chromatography (TLC). The LC-MS/MS profiles of HGs showed the important fragments at m/z ratios of 345.21 (added glucose to glucose of rutinose in HG<sub>1</sub>) and 687.28 (added maltose to glucose of rutinose in HG<sub>2</sub>), confirming that the structures of HG<sub>1</sub> and HG<sub>2</sub> were α-glucosyl hesperidin and α-maltosyl hesperidin, respectively. In addition, <sup>1</sup>H and <sup>13</sup>C-NMR of hesperidin derivatives were performed to identify their α-1,4-glycosidic bonds. The MIC and MBC studies showed that transglycosylated HG<sub>1</sub> and HG<sub>2</sub> had better antibacterial and bactericidal activities than hesperidin and diosmin, and were more active against <i>Staphylococcus aureus</i> than <i>Escherichia coli</i>. Hesperidin, HG<sub>1</sub>, HG<sub>2</sub>, and diosmin inhibited α-glucosidase with IC<sub>50</sub> values of 2.75 ± 1.57, 2.48 ± 1.61, 2.36 ± 1.48, and 2.99 ± 1.23 mg/mL, respectively. The inhibition kinetics of HG<sub>2</sub> shown by a Lineweaver–Burk plot confirmed HG<sub>2</sub> was an α-glucosidase competitive inhibitor with an inhibitor constant, <i>K</i><sub>i</sub>, of 2.20 ± 0.10 mM. Thus, HGs have the potential to be developed into antibacterial drugs and treatments for treating α-glucosidase-associated type 2 diabetes.https://www.mdpi.com/2073-4344/11/5/532chemical structurecyclodextrin glycosyltransferaseantibacterial activityα-glucosidase inhibitionhesperidin glycosides |
| spellingShingle | Titaporn Chaisin Prakarn Rudeekulthamrong Jarunee Kaulpiboon Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin Glycosides Catalysts chemical structure cyclodextrin glycosyltransferase antibacterial activity α-glucosidase inhibition hesperidin glycosides |
| title | Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin Glycosides |
| title_full | Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin Glycosides |
| title_fullStr | Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin Glycosides |
| title_full_unstemmed | Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin Glycosides |
| title_short | Enzymatic Synthesis, Structural Analysis, and Evaluation of Antibacterial Activity and α-Glucosidase Inhibition of Hesperidin Glycosides |
| title_sort | enzymatic synthesis structural analysis and evaluation of antibacterial activity and α glucosidase inhibition of hesperidin glycosides |
| topic | chemical structure cyclodextrin glycosyltransferase antibacterial activity α-glucosidase inhibition hesperidin glycosides |
| url | https://www.mdpi.com/2073-4344/11/5/532 |
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