Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4

© 2018, Chiang Mai University. All rights reserved. Cellulase and xylanase producing bacteria, Bacillus amyloliquefaciens CX1 and Bacillus subtilis B4, were isolated from horse feces and cow’s rumen fluid. Both enzymes were purified, characterized, and determined their molecular weight. The molecula...

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Main Authors: Ratchara Kalawong, Mamoru Wakayama, Somboon Anuntalabhochai, Chalobol Wongsawad, Kanta Sangwijit
Format: Journal
Published: 2018
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http://cmuir.cmu.ac.th/jspui/handle/6653943832/58345
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spelling th-cmuir.6653943832-583452018-09-05T04:39:53Z Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4 Ratchara Kalawong Mamoru Wakayama Somboon Anuntalabhochai Chalobol Wongsawad Kanta Sangwijit Biochemistry, Genetics and Molecular Biology Chemistry Materials Science Mathematics Physics and Astronomy © 2018, Chiang Mai University. All rights reserved. Cellulase and xylanase producing bacteria, Bacillus amyloliquefaciens CX1 and Bacillus subtilis B4, were isolated from horse feces and cow’s rumen fluid. Both enzymes were purified, characterized, and determined their molecular weight. The molecular weight of purified cellulase and xylanase of B. amyloliquefaciens CX1 was found to be 53 kDa and 26 kDa when cellulase and xylanase produced from B. subtilis B4 was estimated to be 46 and 23 kDa, respectively. Both cellulases exhibited their thermostability in wide range of 20-80°C and were stable over a broad range of pH 5-10.While both xylanases showed thermostability ranging 20-50°C, and were stable over a broad pH range of 4.0-9.0. Cellulase and xylanase activities were stimulated by Fe3+, in contrary both enzymes’ activities were strongly inhibited by 10 mM Mn2+and Cu2+. Xylanase from B. amyloliquefaciens CX1 showed the highest hydrolysis activity on various pretreated lignocellulosic substrates including rice straw, corn stover, paragrass and napier grass to total reducing sugar by 2.23, 3.52, 2.72 and 2.39 mg/ml, respectively. Furthermore, cellulase produced from B. subtilis B4 showed maximum release of reducing sugar from napier grass (0.72 mg/ml), followed by paragrass (0.58mg/ml), and rice straw (0.45mg/ml). Cellulase and xylanase produced from B. amyloliquefaciens CX1 and B. subtilis B4 could also be considerable biotechnological interest particularly in fermented food process for cattle feed since the enzymes showed a dramatically stability over broad pH and temperature range. 2018-09-05T04:22:59Z 2018-09-05T04:22:59Z 2018-01-01 Journal 01252526 2-s2.0-85040941724 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85040941724&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/58345
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
topic Biochemistry, Genetics and Molecular Biology
Chemistry
Materials Science
Mathematics
Physics and Astronomy
spellingShingle Biochemistry, Genetics and Molecular Biology
Chemistry
Materials Science
Mathematics
Physics and Astronomy
Ratchara Kalawong
Mamoru Wakayama
Somboon Anuntalabhochai
Chalobol Wongsawad
Kanta Sangwijit
Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4
description © 2018, Chiang Mai University. All rights reserved. Cellulase and xylanase producing bacteria, Bacillus amyloliquefaciens CX1 and Bacillus subtilis B4, were isolated from horse feces and cow’s rumen fluid. Both enzymes were purified, characterized, and determined their molecular weight. The molecular weight of purified cellulase and xylanase of B. amyloliquefaciens CX1 was found to be 53 kDa and 26 kDa when cellulase and xylanase produced from B. subtilis B4 was estimated to be 46 and 23 kDa, respectively. Both cellulases exhibited their thermostability in wide range of 20-80°C and were stable over a broad range of pH 5-10.While both xylanases showed thermostability ranging 20-50°C, and were stable over a broad pH range of 4.0-9.0. Cellulase and xylanase activities were stimulated by Fe3+, in contrary both enzymes’ activities were strongly inhibited by 10 mM Mn2+and Cu2+. Xylanase from B. amyloliquefaciens CX1 showed the highest hydrolysis activity on various pretreated lignocellulosic substrates including rice straw, corn stover, paragrass and napier grass to total reducing sugar by 2.23, 3.52, 2.72 and 2.39 mg/ml, respectively. Furthermore, cellulase produced from B. subtilis B4 showed maximum release of reducing sugar from napier grass (0.72 mg/ml), followed by paragrass (0.58mg/ml), and rice straw (0.45mg/ml). Cellulase and xylanase produced from B. amyloliquefaciens CX1 and B. subtilis B4 could also be considerable biotechnological interest particularly in fermented food process for cattle feed since the enzymes showed a dramatically stability over broad pH and temperature range.
format Journal
author Ratchara Kalawong
Mamoru Wakayama
Somboon Anuntalabhochai
Chalobol Wongsawad
Kanta Sangwijit
author_facet Ratchara Kalawong
Mamoru Wakayama
Somboon Anuntalabhochai
Chalobol Wongsawad
Kanta Sangwijit
author_sort Ratchara Kalawong
title Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4
title_short Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4
title_full Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4
title_fullStr Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4
title_full_unstemmed Comparison and characterization of purified cellulase and Xylanase from bacillus amyloliquefaciens CX1 and bacillus subtilis b4
title_sort comparison and characterization of purified cellulase and xylanase from bacillus amyloliquefaciens cx1 and bacillus subtilis b4
publishDate 2018
url https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85040941724&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/58345
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