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A thermostable alkaline active endo-beta-1-4-xylanase from Bacillus halodurans S7: Purification and characterization

Mamo, Gashaw LU ; Hatti-Kaul, Rajni LU and Mattiasson, Bo LU (2006) In Enzyme and Microbial Technology 39(7). p.1492-1498
Abstract
A thermostable, alkaline active xylanase was purified to homogeneity from the culture supernatant of an alkaliphilic Bacillus halodurans S7, which was isolated from a soda lake in the Ethiopian Rift Valley. The molecular weight and the pI of this enzyme were estimated to be around 43 kDa and 4.5, respectively. When assayed at 70 degrees C, it was optimally active at pH 9.0-9.5. The optimum temperature for the activity was 75 degrees C at pH 9 and 70 degrees C at pH 10. The enzyme was stable over a broad pH range and showed good thermal stability when incubated at 65 degrees C in pH 9 buffer. The enzyme activity was strongly inhibited by Mn2+. Partial inhibition was also observed in the presence of 5 mM Cu2+ Co2+ and EDTA. Inhibition by... (More)
A thermostable, alkaline active xylanase was purified to homogeneity from the culture supernatant of an alkaliphilic Bacillus halodurans S7, which was isolated from a soda lake in the Ethiopian Rift Valley. The molecular weight and the pI of this enzyme were estimated to be around 43 kDa and 4.5, respectively. When assayed at 70 degrees C, it was optimally active at pH 9.0-9.5. The optimum temperature for the activity was 75 degrees C at pH 9 and 70 degrees C at pH 10. The enzyme was stable over a broad pH range and showed good thermal stability when incubated at 65 degrees C in pH 9 buffer. The enzyme activity was strongly inhibited by Mn2+. Partial inhibition was also observed in the presence of 5 mM Cu2+ Co2+ and EDTA. Inhibition by Hg2+ and dithiothreitol was insignificant. The enzyme was free from cellulase activity and degraded xylan in an endo-fashion. (c) 2006 Elsevier Inc. All rights reserved. (Less)
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Contribution to journal
publication status
published
subject
keywords
xylanase, alkaliphile, Bacillus
in
Enzyme and Microbial Technology
volume
39
issue
7
pages
1492 - 1498
publisher
Elsevier
external identifiers
  • wos:000241252100019
  • scopus:33748751574
ISSN
0141-0229
DOI
10.1016/j.enzmictec.2006.03.040
language
English
LU publication?
yes
id
9651807e-3c71-46ad-ad77-d514e8361434 (old id 388093)
date added to LUP
2016-04-01 12:32:15
date last changed
2021-10-03 03:40:42
@article{9651807e-3c71-46ad-ad77-d514e8361434,
  abstract     = {A thermostable, alkaline active xylanase was purified to homogeneity from the culture supernatant of an alkaliphilic Bacillus halodurans S7, which was isolated from a soda lake in the Ethiopian Rift Valley. The molecular weight and the pI of this enzyme were estimated to be around 43 kDa and 4.5, respectively. When assayed at 70 degrees C, it was optimally active at pH 9.0-9.5. The optimum temperature for the activity was 75 degrees C at pH 9 and 70 degrees C at pH 10. The enzyme was stable over a broad pH range and showed good thermal stability when incubated at 65 degrees C in pH 9 buffer. The enzyme activity was strongly inhibited by Mn2+. Partial inhibition was also observed in the presence of 5 mM Cu2+ Co2+ and EDTA. Inhibition by Hg2+ and dithiothreitol was insignificant. The enzyme was free from cellulase activity and degraded xylan in an endo-fashion. (c) 2006 Elsevier Inc. All rights reserved.},
  author       = {Mamo, Gashaw and Hatti-Kaul, Rajni and Mattiasson, Bo},
  issn         = {0141-0229},
  language     = {eng},
  number       = {7},
  pages        = {1492--1498},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {A thermostable alkaline active endo-beta-1-4-xylanase from Bacillus halodurans S7: Purification and characterization},
  url          = {http://dx.doi.org/10.1016/j.enzmictec.2006.03.040},
  doi          = {10.1016/j.enzmictec.2006.03.040},
  volume       = {39},
  year         = {2006},
}