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Sammanfattning

In the present work we suggest an efficient method, using the whole time course of the reaction, whereby parameters k(cat), K-m and product K-I for the hydrolysis of a p-nitrophenyl glycoside by an exo-acting glycoside hydrolase can be estimated in a single experiment. Its applicability was demonstrated for three retaining exo-glycoside hydrolases, beta-xylosidase from Aspergillus awamori, beta-galactosidase from Penicillium sp. and alpha-galactosidase from Thermotoga maritima (TmGalA). During the analysis of the reaction course catalyzed by the TmGalA enzyme we had observed that a non-enzymatic process, mutarotation of the liberated alpha-D-galactose, affected the reaction significantly. (C) 2015 Elsevier Ltd. All rights reserved.

Nyckelord

Integrated kinetics; Retaining glycoside hydrolase; Mutarotation

Publicerad i

Carbohydrate Research
2015, volym: 412, sidor: 43-49
Utgivare: ELSEVIER SCI LTD

SLU författare

  • Borisova, Anna

    • Institutionen för kemi och bioteknologi, Sveriges lantbruksuniversitet
    • National Research Centre - Kurchatov Institute
  • Sandgren, Mats

    • Institutionen för kemi och bioteknologi, Sveriges lantbruksuniversitet

UKÄ forskningsämne

Organisk kemi
Biofysik

Publikationens identifierare

  • DOI: https://doi.org/10.1016/j.carres.2015.03.021

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/68450