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• W1996042866 abstract "α-1,4-Amylase is one of the most important industrial enzymes and there is enormous interest in isolating α-1,4-amylase with better properties. The α-1,4-amylase producing endophytic Bacillus amyloliquefaciens was isolated and characterized from Hevea brasiliensis. The α-1,4-amylase gene after cloning and sequencing contained 1542 base pairs. A homology model of the α-1,4-amylase enzyme was built from the deduced amino acid sequence. The modelled and template α-1,4-amylase enzyme (PDB ID:3bh4) showed 97.7% sequence identity with similar secondary and tertiary structures. Computer aided docking studies of the substrate (maltotetraose) with the modelled as well as the template enzymes showed that although the binding energies were almost the same in both the complexes, the number of hydrogen bonds and van der Waals interactions in the active sites of the two enzymes were different. These variations might be due to the change in the amino acid residues of the active site regions of two enzymes. The mutated p..." @default.
• W1996042866 created "2016-06-24" @default.
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• W1996042866 date "2013-12-01" @default.
• W1996042866 modified "2023-09-24" @default.
• W1996042866 title "Molecular modelling and docking studies of an α-1,4-amylase from endophyticBacillus amyloliquefaciens" @default.
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• W1996042866 doi "https://doi.org/10.1080/21553769.2013.852993" @default.
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