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Lookup NU author(s): Dr Lucy Crouch,
Dr David Bolam
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© 2018 Springer Science+Business Media, LLC, part of Springer Nature A putative GH35 β-galactosidase gene from the mucin-degrading bacterium Akkermansia muciniphila was successfully cloned and further investigated. The recombinant enzyme with the molecular mass of 74 kDa was purified to homogeneity and biochemically characterised. The optimum temperature of the enzyme was 42 °C, and the optimum pH was determined to be pH 3.5. The addition of sodium dodecyl sulphate (SDS) reduced the enzyme’s activity significantly. The addition of Mg2+-ions decreased the activity of the β-galactosidase, whereas other metal ions or EDTA showed no inhibitory effect. The enzyme catalysed the hydrolysis of β1,3- and β1,6- linked galactose residues from various substrates, whereas only negligible amounts of β1,4-galactose were hydrolysed. The present study describes the first functional characterisation of a β-galactosidase from this human gut symbiont.
Author(s): Guo B-S, Zheng F, Crouch L, Cai Z-P, Wang M, Bolam DN, Liu L, Voglmeir J
Publication type: Article
Publication status: Published
Journal: Glycoconjugate Journal
Print publication date: 01/06/2018
Online publication date: 12/05/2018
Acceptance date: 20/04/2018
ISSN (print): 0282-0080
ISSN (electronic): 1573-4986
Publisher: Springer New York LLC
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