Intrinsic dynamic behavior of enzyme:substrate complexes govern the catalytic action of β-galactosidases across clan GH-A
Author:
Funder
Agence Nationale de la Recherche
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-46589-8.pdf
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2. Klein, M. P. et al. High stability of immobilized β-D-galactosidase for lactose hydrolysis and galactooligosaccharides synthesis. Carbohydr. Polym. 95(1), 465–470 (2013).
3. Chen, S. C. & Duan, K. J. Production of galactooligosaccharides using β-galactosidase immobilized on chitosan-coated magnetic nanoparticles with tris(hydroxymethyl)phosphine as an optional coupling agent. Int. J. Mol. Sci. 16, 12499–12512 (2015).
4. Husain, Q. β-Galactosidases and their potential applications: a review. Crit Rev Biotechnol. 30, 41–62 (2010).
5. Lombard, V., Golaconda, R. H., Drula, E., Coutinho, P. M. & Henrissat, B. The Carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 42, 490–495 (2014).
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