Computational docking, molecular dynamics simulation and subsite structure analysis of a maltogenic amylase from Bacillus lehensis G1 provide insights into substrate and product specificity
Maltogenic amylase (MAG1) from Bacillus lehensis G1 displayed the highest hydrolysis activity on β-cyclodextrin (β-CD) to produce maltose as a main product and exhibited high transglycosylation activity on malto-oligosaccharides with polymerization degree of three and above. These substrate and prod...
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Format: | Article |
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Elsevier Inc.
2016
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Online Access: | http://eprints.utm.my/id/eprint/72465/ https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964840632&doi=10.1016%2fj.jmgm.2016.04.004&partnerID=40&md5=352d4a7850681dfca4ca48df8fd8b487 |
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