ePrints

Cloning, purification and biochemical characterisation of a GH35 beta-1,3/beta-1,6-galactosidase from the mucin-degrading gut bacterium Akkermansia muciniphila

Lookup NU author(s): Dr Lucy Crouch, Dr David BolamORCiD

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

© 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.

Publication metadata

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

Year: 2018

Volume: 32

Issue: 3

Pages: 255-263

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

URL: https://doi.org/10.1007/s10719-018-9824-9

DOI: 10.1007/s10719-018-9824-9

Altmetrics

Share