Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory Activities
Arid ecosystems constitute a promising source of actinobacteria producing new bioactive molecules. This study aimed to explore different biological activities of actinomycetes isolated from the rhizosphere of <i>Phoenix dactylifera</i> L. in the Ghardaia region, Algeria. A total of 18 ac...
Saved in:
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-01-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/15/1/65 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832588914004590592 |
|---|---|
| author | Maria Smati Amina Bramki Fatima Zohra Makhlouf Rihab Djebaili Beatrice Farda Fatima Zohra Abdelhadi Nahla Abdelli Mahmoud Kitouni Marika Pellegrini |
| author_facet | Maria Smati Amina Bramki Fatima Zohra Makhlouf Rihab Djebaili Beatrice Farda Fatima Zohra Abdelhadi Nahla Abdelli Mahmoud Kitouni Marika Pellegrini |
| author_sort | Maria Smati |
| collection | DOAJ |
| description | Arid ecosystems constitute a promising source of actinobacteria producing new bioactive molecules. This study aimed to explore different biological activities of actinomycetes isolated from the rhizosphere of <i>Phoenix dactylifera</i> L. in the Ghardaia region, Algeria. A total of 18 actinobacteria were isolated and studied for their enzymatic and antimicrobial activities. All isolates shared cellulase and catalase activity; most of them produced amylase (94%), esterase (84%), lecithinase and lipoproteins (78%), caseinase (94%), and gelatinase (72%). The isolates could coagulate (56%) or peptonize (28%) skim milk. Overall, 72% of the isolates exhibited significant antibacterial activity against at least one test bacteria, while 56% demonstrated antifungal activity against at least one test fungi. Based on enzyme production and antimicrobial activity, isolate SGI16 was selected for secondary metabolite extraction by ethyl acetate. The crude extract of SGI16 was analyzed using DPPH and BSA denaturation inhibition tests, revealing significant antioxidant power (IC<sub>50</sub> = 7.24 ± 0.21 μg mL<sup>−1</sup>) and protein denaturation inhibitory capacity (IC<sub>50</sub> = 492.41 ± 0.47 μg mL<sup>−1</sup>). Molecular identification based on <i>16S rDNA</i> analysis showed that SGI16 belonged to the genus <i>Streptomyces</i>. The findings highlight that date palms’ rhizosphere actinobacteria are a valuable source of biomolecules of biotechnological interest. |
| format | Article |
| id | doaj-art-88f9fd313b7a4819971f8404d7334faa |
| institution | Kabale University |
| issn | 2218-273X |
| language | English |
| publishDate | 2025-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj-art-88f9fd313b7a4819971f8404d7334faa2025-01-24T13:25:02ZengMDPI AGBiomolecules2218-273X2025-01-011516510.3390/biom15010065Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory ActivitiesMaria Smati0Amina Bramki1Fatima Zohra Makhlouf2Rihab Djebaili3Beatrice Farda4Fatima Zohra Abdelhadi5Nahla Abdelli6Mahmoud Kitouni7Marika Pellegrini8Higher National School of Biotechnology Taoufik Khaznadar, Nouveau Pôle Universitaire Ali Mendjeli, BP. E66, Constantine 25100, AlgeriaLaboratory of BioEngineering, Higher National School of Biotechnology Taoufik Khaznadar, Nouveau Pôle Universitaire Ali Mendjeli, BP. E66, Constantine 25100, AlgeriaHigher National School of Biotechnology Taoufik Khaznadar, Nouveau Pôle Universitaire Ali Mendjeli, BP. E66, Constantine 25100, AlgeriaDepartment of Life, Health and Environmental Sciences, University of L’Aquila, Coppito, 67100 L’Aquila, ItalyDepartment of Life, Health and Environmental Sciences, University of L’Aquila, Coppito, 67100 L’Aquila, ItalyHigher National School of Biotechnology Taoufik Khaznadar, Nouveau Pôle Universitaire Ali Mendjeli, BP. E66, Constantine 25100, AlgeriaHigher National School of Biotechnology Taoufik Khaznadar, Nouveau Pôle Universitaire Ali Mendjeli, BP. E66, Constantine 25100, AlgeriaLaboratory of Microbiological Engineering and Applications, University of Brothers Mentouri, Constantine 1, Chaâbat Erssas Campus, Ain El Bey Road, Constantine 25000, AlgeriaDepartment of Life, Health and Environmental Sciences, University of L’Aquila, Coppito, 67100 L’Aquila, ItalyArid ecosystems constitute a promising source of actinobacteria producing new bioactive molecules. This study aimed to explore different biological activities of actinomycetes isolated from the rhizosphere of <i>Phoenix dactylifera</i> L. in the Ghardaia region, Algeria. A total of 18 actinobacteria were isolated and studied for their enzymatic and antimicrobial activities. All isolates shared cellulase and catalase activity; most of them produced amylase (94%), esterase (84%), lecithinase and lipoproteins (78%), caseinase (94%), and gelatinase (72%). The isolates could coagulate (56%) or peptonize (28%) skim milk. Overall, 72% of the isolates exhibited significant antibacterial activity against at least one test bacteria, while 56% demonstrated antifungal activity against at least one test fungi. Based on enzyme production and antimicrobial activity, isolate SGI16 was selected for secondary metabolite extraction by ethyl acetate. The crude extract of SGI16 was analyzed using DPPH and BSA denaturation inhibition tests, revealing significant antioxidant power (IC<sub>50</sub> = 7.24 ± 0.21 μg mL<sup>−1</sup>) and protein denaturation inhibitory capacity (IC<sub>50</sub> = 492.41 ± 0.47 μg mL<sup>−1</sup>). Molecular identification based on <i>16S rDNA</i> analysis showed that SGI16 belonged to the genus <i>Streptomyces</i>. The findings highlight that date palms’ rhizosphere actinobacteria are a valuable source of biomolecules of biotechnological interest.https://www.mdpi.com/2218-273X/15/1/65actinobacteria<i>Phoenix dactylifera</i> L.biomoleculesGhardaiaAlgeria |
| spellingShingle | Maria Smati Amina Bramki Fatima Zohra Makhlouf Rihab Djebaili Beatrice Farda Fatima Zohra Abdelhadi Nahla Abdelli Mahmoud Kitouni Marika Pellegrini Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory Activities Biomolecules actinobacteria <i>Phoenix dactylifera</i> L. biomolecules Ghardaia Algeria |
| title | Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory Activities |
| title_full | Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory Activities |
| title_fullStr | Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory Activities |
| title_full_unstemmed | Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory Activities |
| title_short | Isolation of Actinobacteria from Date Palm Rhizosphere with Enzymatic, Antimicrobial, Antioxidant, and Protein Denaturation Inhibitory Activities |
| title_sort | isolation of actinobacteria from date palm rhizosphere with enzymatic antimicrobial antioxidant and protein denaturation inhibitory activities |
| topic | actinobacteria <i>Phoenix dactylifera</i> L. biomolecules Ghardaia Algeria |
| url | https://www.mdpi.com/2218-273X/15/1/65 |
| work_keys_str_mv | AT mariasmati isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT aminabramki isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT fatimazohramakhlouf isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT rihabdjebaili isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT beatricefarda isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT fatimazohraabdelhadi isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT nahlaabdelli isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT mahmoudkitouni isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities AT marikapellegrini isolationofactinobacteriafromdatepalmrhizospherewithenzymaticantimicrobialantioxidantandproteindenaturationinhibitoryactivities |