Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from <i>Paenibacillus sp.</i>

Md. Abdul High Siddiqui; Mrityunjoy Biswas; Md. Omar Faruk; Manoranjan Roy; A. K. M. Asaduzzaman; Subed Chandra Dev Sharma; Topodeb Biswas; Narayan Roy

doi:doi:10.11648/j.ajls.20160404.11

Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.

Md. Abdul High Siddiqui, Mrityunjoy Biswas, Md. Omar Faruk, Manoranjan Roy, A. K. M. Asaduzzaman, Subed Chandra Dev Sharma, Topodeb Biswas, Narayan Roy

Published in American Journal of Life Sciences (Volume 4, Issue 4)

Received: 2 August 2016 Accepted: 13 August 2016 Published: 29 August 2016

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Abstract

Xylanases are hydrolytic enzymes that cleave the β-1,4-linkage ofwheat bran xylan. For screening of xylanase producing bacteria soil samples were diluted by serial dilution and cultured on selective wheat bran xylan agar media. Two bacterial strains showing clear transparent zone around the colony on xylan agar plate were selected as xylanase producing bacteria. The strain Paenibacillus sp. showed highest xylanolytic activity. The strain was thermophile and produced highly active cellulase free xylanase. The enzyme secretion was enhanced when the medium was supplemented with 0.5% wheat bran xylan, peptone and Ca²⁺ salt. The peak in xylanase production was achieved within 48-60 hours at temperature 50°-55°C and at pH 7.0.The cellulase free xylanase was partially purified by ammonium sulfate fractionation and heat treatment at 50°C. The xylanase was optimally active at pH 7.0 and 55°C; and showed high substrate activity to wheat bran xylan but no activity towards carboxymethylcellulose, cellulose and starch.In future we want to know the structure function relationship of the purified enzyme and also want to known the molecular biological study using highly purified xylanase. For this purpose we have to determine the N-terminal & C-terminal amino acid sequence.

Published in	American Journal of Life Sciences (Volume 4, Issue 4)
DOI	10.11648/j.ajls.20160404.11
Page(s)	93-98
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2016. Published by Science Publishing Group

Keywords

Xylanases, Paenibacillus sp., Cellulose, Xylan, Thermophile, N-terminal & C-terminal Amino Acid Sequence

References

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Md. Abdul High Siddiqui, Mrityunjoy Biswas, Md. Omar Faruk, Manoranjan Roy, A. K. M. Asaduzzaman, et al. (2016). Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.. American Journal of Life Sciences, 4(4), 93-98. https://doi.org/10.11648/j.ajls.20160404.11

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Md. Abdul High Siddiqui; Mrityunjoy Biswas; Md. Omar Faruk; Manoranjan Roy; A. K. M. Asaduzzaman, et al. Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.. Am. J. Life Sci. 2016, 4(4), 93-98. doi: 10.11648/j.ajls.20160404.11

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AMA Style

Md. Abdul High Siddiqui, Mrityunjoy Biswas, Md. Omar Faruk, Manoranjan Roy, A. K. M. Asaduzzaman, et al. Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.. Am J Life Sci. 2016;4(4):93-98. doi: 10.11648/j.ajls.20160404.11

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@article{10.11648/j.ajls.20160404.11,
  author = {Md. Abdul High Siddiqui and Mrityunjoy Biswas and Md. Omar Faruk and Manoranjan Roy and A. K. M. Asaduzzaman and Subed Chandra Dev Sharma and Topodeb Biswas and Narayan Roy},
  title = {Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.},
  journal = {American Journal of Life Sciences},
  volume = {4},
  number = {4},
  pages = {93-98},
  doi = {10.11648/j.ajls.20160404.11},
  url = {https://doi.org/10.11648/j.ajls.20160404.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajls.20160404.11},
  abstract = {Xylanases are hydrolytic enzymes that cleave the β-1,4-linkage ofwheat bran xylan. For screening of xylanase producing bacteria soil samples were diluted by serial dilution and cultured on selective wheat bran xylan agar media. Two bacterial strains showing clear transparent zone around the colony on xylan agar plate were selected as xylanase producing bacteria. The strain Paenibacillus sp. showed highest xylanolytic activity. The strain was thermophile and produced highly active cellulase free xylanase. The enzyme secretion was enhanced when the medium was supplemented with 0.5% wheat bran xylan, peptone and Ca2+ salt. The peak in xylanase production was achieved within 48-60 hours at temperature 50°-55°C and at pH 7.0.The cellulase free xylanase was partially purified by ammonium sulfate fractionation and heat treatment at 50°C. The xylanase was optimally active at pH 7.0 and 55°C; and showed high substrate activity to wheat bran xylan but no activity towards carboxymethylcellulose, cellulose and starch.In future we want to know the structure function relationship of the purified enzyme and also want to known the molecular biological study using highly purified xylanase. For this purpose we have to determine the N-terminal & C-terminal amino acid sequence.},
 year = {2016}
}

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TY - JOUR
T1 - Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.
AU - Md. Abdul High Siddiqui
AU - Mrityunjoy Biswas
AU - Md. Omar Faruk
AU - Manoranjan Roy
AU - A. K. M. Asaduzzaman
AU - Subed Chandra Dev Sharma
AU - Topodeb Biswas
AU - Narayan Roy
Y1 - 2016/08/29
PY - 2016
N1 - https://doi.org/10.11648/j.ajls.20160404.11
DO - 10.11648/j.ajls.20160404.11
T2 - American Journal of Life Sciences
JF - American Journal of Life Sciences
JO - American Journal of Life Sciences
SP - 93
EP - 98
PB - Science Publishing Group
SN - 2328-5737
UR - https://doi.org/10.11648/j.ajls.20160404.11
AB - Xylanases are hydrolytic enzymes that cleave the β-1,4-linkage ofwheat bran xylan. For screening of xylanase producing bacteria soil samples were diluted by serial dilution and cultured on selective wheat bran xylan agar media. Two bacterial strains showing clear transparent zone around the colony on xylan agar plate were selected as xylanase producing bacteria. The strain Paenibacillus sp. showed highest xylanolytic activity. The strain was thermophile and produced highly active cellulase free xylanase. The enzyme secretion was enhanced when the medium was supplemented with 0.5% wheat bran xylan, peptone and Ca2+ salt. The peak in xylanase production was achieved within 48-60 hours at temperature 50°-55°C and at pH 7.0.The cellulase free xylanase was partially purified by ammonium sulfate fractionation and heat treatment at 50°C. The xylanase was optimally active at pH 7.0 and 55°C; and showed high substrate activity to wheat bran xylan but no activity towards carboxymethylcellulose, cellulose and starch.In future we want to know the structure function relationship of the purified enzyme and also want to known the molecular biological study using highly purified xylanase. For this purpose we have to determine the N-terminal & C-terminal amino acid sequence.
VL - 4
IS - 4
ER -

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Author Information

Md. Abdul High Siddiqui

Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh
Mrityunjoy Biswas

Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh
Md. Omar Faruk

Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh
Manoranjan Roy

Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh
A. K. M. Asaduzzaman

Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh
Subed Chandra Dev Sharma

Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh
Topodeb Biswas

Department of Botany, Jahangirnagar University, Savar, Dhaka, Bangladesh
Narayan Roy

Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi, Bangladesh

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Md. Abdul High Siddiqui, Mrityunjoy Biswas, Md. Omar Faruk, Manoranjan Roy, A. K. M. Asaduzzaman, et al. (2016). Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.. American Journal of Life Sciences, 4(4), 93-98. https://doi.org/10.11648/j.ajls.20160404.11

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ACS Style

Md. Abdul High Siddiqui; Mrityunjoy Biswas; Md. Omar Faruk; Manoranjan Roy; A. K. M. Asaduzzaman, et al. Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.. Am. J. Life Sci. 2016, 4(4), 93-98. doi: 10.11648/j.ajls.20160404.11

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AMA Style

Md. Abdul High Siddiqui, Mrityunjoy Biswas, Md. Omar Faruk, Manoranjan Roy, A. K. M. Asaduzzaman, et al. Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.. Am J Life Sci. 2016;4(4):93-98. doi: 10.11648/j.ajls.20160404.11

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@article{10.11648/j.ajls.20160404.11,
  author = {Md. Abdul High Siddiqui and Mrityunjoy Biswas and Md. Omar Faruk and Manoranjan Roy and A. K. M. Asaduzzaman and Subed Chandra Dev Sharma and Topodeb Biswas and Narayan Roy},
  title = {Optimization, Isolation and Characterization of Cellulase–Free Thermostable Xylanase from Paenibacillus sp.},
  journal = {American Journal of Life Sciences},
  volume = {4},
  number = {4},
  pages = {93-98},
  doi = {10.11648/j.ajls.20160404.11},
  url = {https://doi.org/10.11648/j.ajls.20160404.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajls.20160404.11},
  abstract = {Xylanases are hydrolytic enzymes that cleave the β-1,4-linkage ofwheat bran xylan. For screening of xylanase producing bacteria soil samples were diluted by serial dilution and cultured on selective wheat bran xylan agar media. Two bacterial strains showing clear transparent zone around the colony on xylan agar plate were selected as xylanase producing bacteria. The strain Paenibacillus sp. showed highest xylanolytic activity. The strain was thermophile and produced highly active cellulase free xylanase. The enzyme secretion was enhanced when the medium was supplemented with 0.5% wheat bran xylan, peptone and Ca2+ salt. The peak in xylanase production was achieved within 48-60 hours at temperature 50°-55°C and at pH 7.0.The cellulase free xylanase was partially purified by ammonium sulfate fractionation and heat treatment at 50°C. The xylanase was optimally active at pH 7.0 and 55°C; and showed high substrate activity to wheat bran xylan but no activity towards carboxymethylcellulose, cellulose and starch.In future we want to know the structure function relationship of the purified enzyme and also want to known the molecular biological study using highly purified xylanase. For this purpose we have to determine the N-terminal & C-terminal amino acid sequence.},
 year = {2016}
}

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