Abstract
Mannan-degrading enzymes have been growing interest in bio-industrial applications, such as the pulp and paper, food, and pharmaceutical industries. In this study, an extremely alkaline mannanase (MnB31) is produced by Bacillus subtilis subsp. inaquosorum CSB31. MnB31 is purified to 17.92-fold with a 21.51% yield and specific activity of 1,796.13Umg-1 by anion-exchange and gel filtration column chromatography. The biochemical characterization of MnB31 is performed, and the results are as follows: molecular weight of ≈47kDa with an optimum temperature of 60°C and pH of 12.5. The enzyme is strongly activated by Co2+, Mn2+, Na+, and K+, and inhibited by Zn2+, Ni2+, and Mg2+. Halo-tolerance (10% NaCl), urea stability (3M), and protease resistance are also observed. The kinetic parameters of MnB31 are found to be Km of 0.043mgml-1, and Vmax of 1,046±3.605Umg-1, respectively. In addition, the thermodynamical parameters are investigated; the activation energy (Ea) is found to be 31.36kJmol-1 with a Kcat value of 156.9×104s-1, ΔH (28.59kJmol-1), ΔG (42.38kJmol-1), ΔS (-41.39Jmol-1K-1), Q10 (1.40), ΔGE-S (-8.697kJmol-1), and ΔGE-T (-48.22kJmol-1). These results suggest that MnB31 has potential bio-industrial application, due to its greater hydrolytic efficiency and feasibility of enzymatic reaction.
| Original language | English |
|---|---|
| Journal | Biotechnology Journal |
| DOIs | |
| Publication status | Accepted/In press - 2017 |
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Keywords
- Bacillus subtilis
- Bioindustry
- Lignocellulose
- Mannanase
- Thermodynamic characterization
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Molecular Medicine
Cite this
Prospects for Bio-Industrial Application of an Extremely Alkaline Mannanase From Bacillus subtilis subsp. inaquosorum CSB31. / Regmi, Sudip; Yoo, Hah Y.; Choi, Yun H.; Choi, Yoon S.; Yoo, Jin C.; Kim, Seung Wook.
In: Biotechnology Journal, 2017.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Prospects for Bio-Industrial Application of an Extremely Alkaline Mannanase From Bacillus subtilis subsp. inaquosorum CSB31
AU - Regmi, Sudip
AU - Yoo, Hah Y.
AU - Choi, Yun H.
AU - Choi, Yoon S.
AU - Yoo, Jin C.
AU - Kim, Seung Wook
PY - 2017
Y1 - 2017
N2 - Mannan-degrading enzymes have been growing interest in bio-industrial applications, such as the pulp and paper, food, and pharmaceutical industries. In this study, an extremely alkaline mannanase (MnB31) is produced by Bacillus subtilis subsp. inaquosorum CSB31. MnB31 is purified to 17.92-fold with a 21.51% yield and specific activity of 1,796.13Umg-1 by anion-exchange and gel filtration column chromatography. The biochemical characterization of MnB31 is performed, and the results are as follows: molecular weight of ≈47kDa with an optimum temperature of 60°C and pH of 12.5. The enzyme is strongly activated by Co2+, Mn2+, Na+, and K+, and inhibited by Zn2+, Ni2+, and Mg2+. Halo-tolerance (10% NaCl), urea stability (3M), and protease resistance are also observed. The kinetic parameters of MnB31 are found to be Km of 0.043mgml-1, and Vmax of 1,046±3.605Umg-1, respectively. In addition, the thermodynamical parameters are investigated; the activation energy (Ea) is found to be 31.36kJmol-1 with a Kcat value of 156.9×104s-1, ΔH (28.59kJmol-1), ΔG (42.38kJmol-1), ΔS (-41.39Jmol-1K-1), Q10 (1.40), ΔGE-S (-8.697kJmol-1), and ΔGE-T (-48.22kJmol-1). These results suggest that MnB31 has potential bio-industrial application, due to its greater hydrolytic efficiency and feasibility of enzymatic reaction.
AB - Mannan-degrading enzymes have been growing interest in bio-industrial applications, such as the pulp and paper, food, and pharmaceutical industries. In this study, an extremely alkaline mannanase (MnB31) is produced by Bacillus subtilis subsp. inaquosorum CSB31. MnB31 is purified to 17.92-fold with a 21.51% yield and specific activity of 1,796.13Umg-1 by anion-exchange and gel filtration column chromatography. The biochemical characterization of MnB31 is performed, and the results are as follows: molecular weight of ≈47kDa with an optimum temperature of 60°C and pH of 12.5. The enzyme is strongly activated by Co2+, Mn2+, Na+, and K+, and inhibited by Zn2+, Ni2+, and Mg2+. Halo-tolerance (10% NaCl), urea stability (3M), and protease resistance are also observed. The kinetic parameters of MnB31 are found to be Km of 0.043mgml-1, and Vmax of 1,046±3.605Umg-1, respectively. In addition, the thermodynamical parameters are investigated; the activation energy (Ea) is found to be 31.36kJmol-1 with a Kcat value of 156.9×104s-1, ΔH (28.59kJmol-1), ΔG (42.38kJmol-1), ΔS (-41.39Jmol-1K-1), Q10 (1.40), ΔGE-S (-8.697kJmol-1), and ΔGE-T (-48.22kJmol-1). These results suggest that MnB31 has potential bio-industrial application, due to its greater hydrolytic efficiency and feasibility of enzymatic reaction.
KW - Bacillus subtilis
KW - Bioindustry
KW - Lignocellulose
KW - Mannanase
KW - Thermodynamic characterization
UR - http://www.scopus.com/inward/record.url?scp=85030107246&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85030107246&partnerID=8YFLogxK
U2 - 10.1002/biot.201700113
DO - 10.1002/biot.201700113
M3 - Article
C2 - 28843040
AN - SCOPUS:85030107246
JO - Biotechnology Journal
JF - Biotechnology Journal
SN - 1860-6768
ER -