Autor: |
Ramanathan N; Department of Zoology, University of Madras, Chennai, India., Sreeramulu B; Department of Zoology, University of Madras, Chennai, India., Mani M; Department of Zoology, University of Madras, Chennai, India., Sundaram J; Department of Zoology, University of Madras, Chennai, India. |
Jazyk: |
angličtina |
Zdroj: |
Natural product research [Nat Prod Res] 2024 Dec; Vol. 38 (23), pp. 4146-4154. Date of Electronic Publication: 2023 Nov 15. |
DOI: |
10.1080/14786419.2023.2280169 |
Abstrakt: |
Insects possess cellulolytic system capable of producing variegate enzymes with multifarious specificities to break down complex lignocellulosic products. Astonishingly, endoglucanases, exoglucanases and β-glycosidases act sequentially in a synergistic system to facilitate the breakdown of cellulose to utilisable energy source glucose. In silico docking studies of endo-β-1,4-glucanase from 19 different insects belonging to six different orders identified that it possesses high affinity for all the six substrates, including CMC, cellulose, cellotriose, cellotetraose, cellopentose and cellohexaose. Additionally, β-glucosidase from nearly all the reported insect sources also showed considerable affinity towards cellobiose. Van der Waals, conventional hydrogen bonds and carbon-hydrogen bonds stabilise the interaction between the enzyme and different substrates. Molecular dynamics simulations also held up the stability of various complexes. Efficient breakdown of lignocelluloses-based substrates becoming a major focus of industrial and academic communities worldwide, this study can perhaps complement the propensity of insect cellulases for prospected applications. |
Databáze: |
MEDLINE |
Externí odkaz: |
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