| Autor: |
Singh PK; Enzyme Technology and Protein Bioinformatics Laboratory, Department of Microbiology, Maharshi Dayanand University, Rohtak, Haryana, India., Joseph J; Enzyme Technology and Protein Bioinformatics Laboratory, Department of Microbiology, Maharshi Dayanand University, Rohtak, Haryana, India., Goyal S; School of Biotechnology, Jawaharlal Nehru University, New Delhi, 110067, India., Grover A; School of Biotechnology, Jawaharlal Nehru University, New Delhi, 110067, India., Shukla P; Enzyme Technology and Protein Bioinformatics Laboratory, Department of Microbiology, Maharshi Dayanand University, Rohtak, Haryana, India. pratyoosh.shukla@gmail.com. |
| Abstrakt: |
Recently inulinase has regained interest due to its usage in the production of fructooligosaccharides, biofuels, and in pharmaceutical industries. Inulinases properties are experimentally reported by nomerous studies but their characteristics are just partially explained by only a few computational investigations. In the present study we have investigated exoinulinase and endoinulinase from different microbial sources toward their catalytic activity. Docking and molecular dynamic (MD) simulation were carried out for microbial endoinulinase and exoinulinase docked with 1-kestose and fructose-6-phosphate respectively. Pseudomonas mucidolens (-7.42 kcal mol(-1) binding energy), docked with fructose-6-phosphate, was recorded as the most favorable binding energy, Pseudomonas mucidolens made hydrogen bonds with fructose-6-phosphate and the amino acids involved were arginine 286, tryptophan 158, and isoleucine 87. After the simulation only tryptophan 158 remained bonded and additionally valine 156 made hydrogen bonds with fructose-6-phosphate. Aspergillus niger docked with 1-kestose was bonded with the involvement of threonine 271, aspartate 285, threonine 288, and proline 283, after the simulation aspartate 285 was retained till the end of the simulation. The present study thus refers to the indication of depicting binding analysis of microbial inulinases. |
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