Issue 28, 2016

Bio-chemical characterization of a β-mannanase from Bacillus licheniformis HDYM-04 isolated from flax water-retting liquid and its decolorization ability of dyes

Abstract

A β-mannanase was purified from the bacteria, Bacillus licheniformis HDYM-04, which was a high β-mannanase-producing strain (576.16 U mL−1 at 48 h during fermentation). The optimal temperature and pH for this enzyme activity were 60 °C and 8.0, respectively. The enzyme activity was significantly enhanced by Co2+, Mg2+, K+, Ba2+ and Na+ while inhibited by β-mercaptoethanol, DTT, SDS, Tween and EDTA. It was also noticed that the enzyme did not lose its activity in a wide interval such as high NaCl concentration (5 mol L−1) and high urea concentration (5 mol L−1). When amino acid residues were modified with NEM, N-AI and NBS, the enzyme activities significantly decreased. CD spectra demonstrated that the secondary structure of β-mannanase consists of 0% α-helix, 27.9% β-sheet, 24.4% turn and 47.7% random coil. CD spectra also supported that β-mannanase was stable under temperature and pH variation. Ten structurally different dyes could be effectively decolorized by β-mannanase within 24 h, in which Congo red (100%), malachite green (100%), titan yellow (98.6%) and phenol red (91%) had high decolorization rates. This property showed the compound's potential application in textile and paper-making industries to decolorize redundant dyes on them.

Graphical abstract: Bio-chemical characterization of a β-mannanase from Bacillus licheniformis HDYM-04 isolated from flax water-retting liquid and its decolorization ability of dyes

Article information

Article type
Paper
Submitted
09 Dec 2015
Accepted
25 Feb 2016
First published
26 Feb 2016

RSC Adv., 2016,6, 23612-23621

Author version available

Bio-chemical characterization of a β-mannanase from Bacillus licheniformis HDYM-04 isolated from flax water-retting liquid and its decolorization ability of dyes

J. P. Ge, R. P. Du, D. Zhao, G. Song, M. Jin and W. X. Ping, RSC Adv., 2016, 6, 23612 DOI: 10.1039/C5RA25888J

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements