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Discovery of a Bacterial Glycoside Hydrolase Family 3 (GH3) ?-Glucosidase with Myrosinase Activity from aCitrobacterStrain Isolated from Soil

Albaser, Abdulhadi, Kazana, Eleanna, Bennett, Mark H., Cebeci, Fatma, Luang-In, Vijitra, Spanu, Pietro D., Rossiter, John T. (2016) Discovery of a Bacterial Glycoside Hydrolase Family 3 (GH3) ?-Glucosidase with Myrosinase Activity from aCitrobacterStrain Isolated from Soil. Journal of Agricultural and Food Chemistry, 64 (7). pp. 1520-1527. ISSN 0021-8561. (doi:10.1021/acs.jafc.5b05381) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
https://doi.org/10.1021/acs.jafc.5b05381

Abstract

A Citrobacter strain (WYE1) was isolated from a UK soil by enrichment using the glucosinolate sinigrin as sole carbon source. The enzyme myrosinase was purified using a combination of ion exchange and gel filtration to give a pure protein of approximately 66 kDa. The N-terminal amino acid and internal peptide sequence of the purified protein were determined and used to identify the gene, which, based on InterPro sequence analysis, belongs to the family GH3, contains a signal peptide, and is a periplasmic protein with a predicted molecular mass of 71.8 kDa. A preliminary characterization was carried out using protein extracts from cell-free preparations. The apparent KM and Vmax were 0.46 mM and 4.91 mmol dm–3 min–1 mg–1, respectively, with sinigrin as substrate. The optimum temperature and pH for enzyme activity were 25 °C and 6.0, respectively. The enzyme was marginally activated with ascorbate by a factor of 1.67.

Item Type: Article
DOI/Identification number: 10.1021/acs.jafc.5b05381
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: E. Kazana
Date Deposited: 03 Mar 2017 15:23 UTC
Last Modified: 29 May 2019 18:46 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/60703 (The current URI for this page, for reference purposes)
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