Purification and Characterization of Linamarse from Gadung (Dioscorea hispida Dennst) for Gadung Slurry Detoxification

Authors

  • Harijono Harijono
  • Siwi N.
  • Aji Sutrisno

Abstract

The aim of this research was to find out purification of enzyme linamarase fromDioscorea hispida Dennts. Enzyme purification was carried out by amonium sulphatefractionation and Sephadex G-75 gel filtration coloumn chromatography. Protein purifyfactor achieved was 10.5 times, protein yield was 33.3 % of the crude cell extract proteinand specific activity was 2.93 U/mg. The enzyme purity of each purification stage wasmonitored by SDS-PAGE and resulted one protein band. The optimum temperature andpH of enzyme reaction was 57°C and pH 6.5 with 90 minutes incubation. Using crudelinamarin as substrat, linamarase has Km 0.1564 μmol ml and Vmax 0.2796μmol/minute. Pure linamarase was added in Dioscorea slurry to increase cyaniderelease.

 

Keywords: purification, characterization, linamarase, detoxification, Dioscorea hispidaDennts.

Downloads

Published

2012-01-25

Issue

Vol. 12 No. 2 (2011)

Section

Articles

License

Authors who publish with this journal agree to the following terms:

    1. Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal
    2. Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal