Prospects for Bio-Industrial Application of an Extremely Alkaline Mannanase From Bacillus subtilis subsp. inaquosorum CSB31

Sudip Regmi, Hah Y. Yoo, Yun H. Choi, Yoon S. Choi, Jin C. Yoo, Seung Wook Kim

Research output: Contribution to journalArticle

10 Citations (Scopus)

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 languageEnglish
JournalBiotechnology Journal
DOIs
Publication statusAccepted/In press - 2017

Fingerprint

Bacillus subtilis
Mannans
Food Industry
Drug Industry
Enzymes
Gel Chromatography
Anions
Urea
Peptide Hydrolases
Molecular Weight
Temperature

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 journalArticle

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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.",
keywords = "Bacillus subtilis, Bioindustry, Lignocellulose, Mannanase, Thermodynamic characterization",
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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

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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.

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KW - Bioindustry

KW - Lignocellulose

KW - Mannanase

KW - Thermodynamic characterization

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