An examination of the microbiome of Bacillus cereus (PS5) isolated from Puntius sarana (Olive barb) for α-amylase production, optimization, macromolecule extraction, and structural characterization with industrial and agricultural applications.
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| Format: | Artículo científico |
| Langue: | en |
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International journal of biological macromolecules
2026
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| author | Dhayalan, Arul Manoharan, Sumathi Waheeb, Mohammed Qasim Rabbee, Muhammad Fazle Govindasamy, Balasubramani Selvan, Silambarasan Tamil Pachiappan, Perumal |
| author_facet | Dhayalan, Arul Manoharan, Sumathi Waheeb, Mohammed Qasim Rabbee, Muhammad Fazle Govindasamy, Balasubramani Selvan, Silambarasan Tamil Pachiappan, Perumal Dhayalan, Arul Manoharan, Sumathi Waheeb, Mohammed Qasim Rabbee, Muhammad Fazle Govindasamy, Balasubramani Selvan, Silambarasan Tamil Pachiappan, Perumal |
| collection | PubMed - marine biology |
| contents | An examination of the microbiome of Bacillus cereus (PS5) isolated from Puntius sarana (Olive barb) for α-amylase production, optimization, macromolecule extraction, and structural characterization with industrial and agricultural applications. Dhayalan, Arul Manoharan, Sumathi Waheeb, Mohammed Qasim Rabbee, Muhammad Fazle Govindasamy, Balasubramani Selvan, Silambarasan Tamil Pachiappan, Perumal Bacillus cereus alpha-Amylases Animals Molecular Docking Simulation Hydrogen-Ion Concentration Bacterial Proteins Temperature Molecular Weight The α-amylase enzyme plays a vital role in enzyme therapy and the intestinal digestive system, and is widely utilized in the food and pharmaceutical industries. Thus, this study aimed to isolate intestinal bacterial strains that produce α-amylase, optimize enzyme production, and characterize the molecular properties of the produced proteins. A total of 11 strains were isolated from the fish gut; 9 strains were positive for α-amylase production. The PS5 strain exhibited the highest enzymatic activity and was confirmed as Bacillus cereus. Optimization of B. cereus culture conditions revealed parameters of pH 7.0, temperature 35 °C, incubation time 40 h, and starch and yeast extracts of 1.5% and 2.53%, respectively. The bacterial protein was extracted, purified, and shown to have a molecular weight of 55 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. FTIR spectroscopy confirmed the presence of functional groups, such as phenols, alkanes, amides, and aromatic and aliphatic amines. Matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF)-tandem mass spectrometry (MS/MS) analysis identified 12 peptides, with the major peptide sequence being SVGLLLVLLLPMLGAAAPLTTQMLDSGWQFR (m/z 2383.97; S/N 69.3). The α-amylase protein sequence (513 amino acids) was used for structural prediction, while protein-protein interaction analysis revealed a significant interaction with pullulanase (interaction score 0.945). Molecular docking analysis showed strong binding energy of propoxur (-7.2 kcal/mol) and the hormone indole-3-acetic acid (-6.9 kcal/mol) with α-amylase protein. These findings indicate that Bacillus cereus (PS5) is a promising source of α-amylase for diverse industrial and agricultural applications. Further investigation into the activity and stability of these enzymes in natural environments could enhance the associated potential biotechnological applications. |
| format | Artículo científico |
| id | pubmed_42103122 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | International journal of biological macromolecules |
| record_format | pubmed |
| spellingShingle | An examination of the microbiome of Bacillus cereus (PS5) isolated from Puntius sarana (Olive barb) for α-amylase production, optimization, macromolecule extraction, and structural characterization with industrial and agricultural applications. Dhayalan, Arul Manoharan, Sumathi Waheeb, Mohammed Qasim Rabbee, Muhammad Fazle Govindasamy, Balasubramani Selvan, Silambarasan Tamil Pachiappan, Perumal Bacillus cereus alpha-Amylases Animals Molecular Docking Simulation Hydrogen-Ion Concentration Bacterial Proteins Temperature Molecular Weight An examination of the microbiome of Bacillus cereus (PS5) isolated from Puntius sarana (Olive barb) for α-amylase production, optimization, macromolecule extraction, and structural characterization with industrial and agricultural applications. Dhayalan, Arul Manoharan, Sumathi Waheeb, Mohammed Qasim Rabbee, Muhammad Fazle Govindasamy, Balasubramani Selvan, Silambarasan Tamil Pachiappan, Perumal Bacillus cereus alpha-Amylases Animals Molecular Docking Simulation Hydrogen-Ion Concentration Bacterial Proteins Temperature Molecular Weight The α-amylase enzyme plays a vital role in enzyme therapy and the intestinal digestive system, and is widely utilized in the food and pharmaceutical industries. Thus, this study aimed to isolate intestinal bacterial strains that produce α-amylase, optimize enzyme production, and characterize the molecular properties of the produced proteins. A total of 11 strains were isolated from the fish gut; 9 strains were positive for α-amylase production. The PS5 strain exhibited the highest enzymatic activity and was confirmed as Bacillus cereus. Optimization of B. cereus culture conditions revealed parameters of pH 7.0, temperature 35 °C, incubation time 40 h, and starch and yeast extracts of 1.5% and 2.53%, respectively. The bacterial protein was extracted, purified, and shown to have a molecular weight of 55 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. FTIR spectroscopy confirmed the presence of functional groups, such as phenols, alkanes, amides, and aromatic and aliphatic amines. Matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF)-tandem mass spectrometry (MS/MS) analysis identified 12 peptides, with the major peptide sequence being SVGLLLVLLLPMLGAAAPLTTQMLDSGWQFR (m/z 2383.97; S/N 69.3). The α-amylase protein sequence (513 amino acids) was used for structural prediction, while protein-protein interaction analysis revealed a significant interaction with pullulanase (interaction score 0.945). Molecular docking analysis showed strong binding energy of propoxur (-7.2 kcal/mol) and the hormone indole-3-acetic acid (-6.9 kcal/mol) with α-amylase protein. These findings indicate that Bacillus cereus (PS5) is a promising source of α-amylase for diverse industrial and agricultural applications. Further investigation into the activity and stability of these enzymes in natural environments could enhance the associated potential biotechnological applications. |
| title | An examination of the microbiome of Bacillus cereus (PS5) isolated from Puntius sarana (Olive barb) for α-amylase production, optimization, macromolecule extraction, and structural characterization with industrial and agricultural applications. |
| topic | Bacillus cereus alpha-Amylases Animals Molecular Docking Simulation Hydrogen-Ion Concentration Bacterial Proteins Temperature Molecular Weight |
| url | https://pubmed.ncbi.nlm.nih.gov/42103122/ |