We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost.
- Authors
Taibi, Zina; Saoudi, Boudjemaa; Boudelaa, Mokhtar; Trigui, Héla; Belghith, Hafedh; Gargouri, Ali; Ladjama, Ali
- Abstract
An extracellular thermostable xylanase from a newly isolated thermophilic Actinomadura sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption-ionization time-of-flight mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5-10 and up to a temperature of 90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C were 2 and 1 h, respectively. The xylanase was specific for xylans, showing higher specific activity on soluble oat-spelt xylan followed by beechwood xylan. This enzyme obeyed the Michaelis-Menten kinetics, with the K and k values being 1.55 mg soluble oat-spelt xylan/ml and 388 min, respectively. While the xylanase from Actinomadura sp. Cpt20 was activated by Mn, Ca, and Cu, it was, strongly inhibited by Hg, Zn, and Ba. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in the pulp and paper industry.
- Subjects
ACTINOMADURA; XYLANASES; IONIZATION (Atomic physics); ENZYMES; PAPER industry
- Publication
Applied Biochemistry & Biotechnology, 2012, Vol 166, Issue 3, p663
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-011-9457-y