Characterization of mannanase from Bacillus circulans NT 6.7 and its application in mannooligosaccharides preparation as prebiotic

This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of...

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Published inSpringerPlus Vol. 4; no. 1; pp. 771 - 11
Main Authors Pangsri, Phanwipa, Piwpankaew, Yotthachai, Ingkakul, Arunee, Nitisinprasert, Sunee, Keawsompong, Suttipun
Format Journal Article
LanguageEnglish
Published Cham Springer International Publishing 14.12.2015
Springer Nature B.V
Subjects
Bacillus circulans
Biomedical and Life Sciences
Carbon sources
Humanities and Social Sciences
Lactobacillus
multidisciplinary
Salmonella enterica
Science
Science (multidisciplinary)
Shigella
Staphylococcus aureus
Ultrafiltration
Defatted copra meal
Mannooligosaccharides
Mannanase
Prebiotics
Bacillus circulans
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Abstract This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of Q-Sepharose. The purified protein (M1) was a dimeric protein with a 40 kDa subunit. The purified M1 exhibited optimum pH and temperature at pH 6.0 and 60 °C, respectively. It was activated by Mn 2+, Mg 2+, and Cu 2+ , and as inhibited by EDTA (45–65 %). The purified enzyme exhibited high specificity to beta-mannan: konjac (glucomannan), locust bean gum (galactomannan), ivory nut (mannan), guar gum (galactomannan) and defatted copra meal (galactomannan). The defatted copra meal could be hydrolyzed by purified M1 into mannooligosaccharides which promoted beneficial bacteria, especially Lactobacillus group, and inhibited pathogenic bacteria; Shigella dysenteria DMST 1511, Staphylococcus aureus TISTR 029, and Salmonella enterica serovar Enteritidis DMST 17368. Therefore, the mannanase from B. circulans NT 6.7 would be a novel source of enzymes for the mannooligosaccharides production as prebiotics.
AbstractList This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of Q-Sepharose. The purified protein (M1) was a dimeric protein with a 40 kDa subunit. The purified M1 exhibited optimum pH and temperature at pH 6.0 and 60 °C, respectively. It was activated by Mn(2+,) Mg(2+,) and Cu(2+), and as inhibited by EDTA (45-65 %). The purified enzyme exhibited high specificity to beta-mannan: konjac (glucomannan), locust bean gum (galactomannan), ivory nut (mannan), guar gum (galactomannan) and defatted copra meal (galactomannan). The defatted copra meal could be hydrolyzed by purified M1 into mannooligosaccharides which promoted beneficial bacteria, especially Lactobacillus group, and inhibited pathogenic bacteria; Shigella dysenteria DMST 1511, Staphylococcus aureus TISTR 029, and Salmonella enterica serovar Enteritidis DMST 17368. Therefore, the mannanase from B. circulans NT 6.7 would be a novel source of enzymes for the mannooligosaccharides production as prebiotics.
This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of Q-Sepharose. The purified protein (M1) was a dimeric protein with a 40 kDa subunit. The purified M1 exhibited optimum pH and temperature at pH 6.0 and 60 °C, respectively. It was activated by Mn 2+, Mg 2+, and Cu 2+ , and as inhibited by EDTA (45–65 %). The purified enzyme exhibited high specificity to beta-mannan: konjac (glucomannan), locust bean gum (galactomannan), ivory nut (mannan), guar gum (galactomannan) and defatted copra meal (galactomannan). The defatted copra meal could be hydrolyzed by purified M1 into mannooligosaccharides which promoted beneficial bacteria, especially Lactobacillus group, and inhibited pathogenic bacteria; Shigella dysenteria DMST 1511, Staphylococcus aureus TISTR 029, and Salmonella enterica serovar Enteritidis DMST 17368. Therefore, the mannanase from B. circulans NT 6.7 would be a novel source of enzymes for the mannooligosaccharides production as prebiotics.
This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of Q-Sepharose. The purified protein (M1) was a dimeric protein with a 40 kDa subunit. The purified M1 exhibited optimum pH and temperature at pH 6.0 and 60 °C, respectively. It was activated by Mn(2+,) Mg(2+,) and Cu(2+), and as inhibited by EDTA (45-65 %). The purified enzyme exhibited high specificity to beta-mannan: konjac (glucomannan), locust bean gum (galactomannan), ivory nut (mannan), guar gum (galactomannan) and defatted copra meal (galactomannan). The defatted copra meal could be hydrolyzed by purified M1 into mannooligosaccharides which promoted beneficial bacteria, especially Lactobacillus group, and inhibited pathogenic bacteria; Shigella dysenteria DMST 1511, Staphylococcus aureus TISTR 029, and Salmonella enterica serovar Enteritidis DMST 17368. Therefore, the mannanase from B. circulans NT 6.7 would be a novel source of enzymes for the mannooligosaccharides production as prebiotics.This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of Q-Sepharose. The purified protein (M1) was a dimeric protein with a 40 kDa subunit. The purified M1 exhibited optimum pH and temperature at pH 6.0 and 60 °C, respectively. It was activated by Mn(2+,) Mg(2+,) and Cu(2+), and as inhibited by EDTA (45-65 %). The purified enzyme exhibited high specificity to beta-mannan: konjac (glucomannan), locust bean gum (galactomannan), ivory nut (mannan), guar gum (galactomannan) and defatted copra meal (galactomannan). The defatted copra meal could be hydrolyzed by purified M1 into mannooligosaccharides which promoted beneficial bacteria, especially Lactobacillus group, and inhibited pathogenic bacteria; Shigella dysenteria DMST 1511, Staphylococcus aureus TISTR 029, and Salmonella enterica serovar Enteritidis DMST 17368. Therefore, the mannanase from B. circulans NT 6.7 would be a novel source of enzymes for the mannooligosaccharides production as prebiotics.
This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of Q-Sepharose. The purified protein (M1) was a dimeric protein with a 40 kDa subunit. The purified M1 exhibited optimum pH and temperature at pH 6.0 and 60 °C, respectively. It was activated by Mn 2+, Mg2+, and Cu2+, and as inhibited by EDTA (45-65 %). The purified enzyme exhibited high specificity to beta-mannan: konjac (glucomannan), locust bean gum (galactomannan), ivory nut (mannan), guar gum (galactomannan) and defatted copra meal (galactomannan). The defatted copra meal could be hydrolyzed by purified M1 into mannooligosaccharides which promoted beneficial bacteria, especially Lactobacillus group, and inhibited pathogenic bacteria; Shigella dysenteria DMST 1511, Staphylococcus aureus TISTR 029, and Salmonella enterica serovar Enteritidis DMST 17368. Therefore, the mannanase from B. circulans NT 6.7 would be a novel source of enzymes for the mannooligosaccharides production as prebiotics.
This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans NT 6.7 was produced using defatted copra meal as a carbon source. The mannanase was purified by ultrafiltration and column chromatography of Q-Sepharose. The purified protein (M1) was a dimeric protein with a 40 kDa subunit. The purified M1 exhibited optimum pH and temperature at pH 6.0 and 60 degree C, respectively. It was activated by Mn super(2+,) Mg super(2+,) and Cu super(2+), and as inhibited by EDTA (45-65 %). The purified enzyme exhibited high specificity to beta-mannan: konjac (glucomannan), locust bean gum (galactomannan), ivory nut (mannan), guar gum (galactomannan) and defatted copra meal (galactomannan). The defatted copra meal could be hydrolyzed by purified M1 into mannooligosaccharides which promoted beneficial bacteria, especially Lactobacillus group, and inhibited pathogenic bacteria; Shigella dysenteria DMST 1511, Staphylococcus aureus TISTR 029, and Salmonella enterica serovar Enteritidis DMST 17368. Therefore, the mannanase from B. circulans NT 6.7 would be a novel source of enzymes for the mannooligosaccharides production as prebiotics.
ArticleNumber 771
Author Piwpankaew, Yotthachai
Ingkakul, Arunee
Nitisinprasert, Sunee
Keawsompong, Suttipun
Pangsri, Phanwipa
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  surname: Pangsri
  fullname: Pangsri, Phanwipa
  organization: Department of Biotechnology, Faculty of Agro-Industry, Kasetsart University
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  givenname: Yotthachai
  surname: Piwpankaew
  fullname: Piwpankaew, Yotthachai
  organization: Interdisciplinary Program in Genetic Engineering, Graduate School, Kasetsart University, Special Research Unit: Probiotic and Prebiotics for Health, Center for Advanced Studies for Agriculture and Food (CASAF), Institute for Advanced Studies, Kasetsart University
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  surname: Ingkakul
  fullname: Ingkakul, Arunee
  organization: Department of Biochemistry, Faculty of Science, Kasetsart University
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  givenname: Sunee
  surname: Nitisinprasert
  fullname: Nitisinprasert, Sunee
  organization: Department of Biotechnology, Faculty of Agro-Industry, Kasetsart University, Interdisciplinary Program in Genetic Engineering, Graduate School, Kasetsart University, Special Research Unit: Probiotic and Prebiotics for Health, Center for Advanced Studies for Agriculture and Food (CASAF), Institute for Advanced Studies, Kasetsart University, Center for Agricultural Biotechnology (CAB), Kasetsart University
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  organization: Department of Biotechnology, Faculty of Agro-Industry, Kasetsart University, Interdisciplinary Program in Genetic Engineering, Graduate School, Kasetsart University, Special Research Unit: Probiotic and Prebiotics for Health, Center for Advanced Studies for Agriculture and Food (CASAF), Institute for Advanced Studies, Kasetsart University, Center for Agricultural Biotechnology (CAB), Kasetsart University
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Issue 1
Keywords Defatted copra meal
Mannooligosaccharides
Mannanase
Prebiotics
Bacillus circulans
Language English
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K Phothichitto (1565_CR15) 2006; 40
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M Zhang (1565_CR20) 2009; 83
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Snippet This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans...
This study focused on the characterization of mannanase from Bacillus circulans NT 6.7 for mannooligosaccharides (MOS) production. The enzyme from B. circulans...
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SubjectTerms Bacillus circulans
Biomedical and Life Sciences
Carbon sources
Humanities and Social Sciences
Lactobacillus
multidisciplinary
Salmonella enterica
Science
Science (multidisciplinary)
Shigella
Staphylococcus aureus
Ultrafiltration
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Title Characterization of mannanase from Bacillus circulans NT 6.7 and its application in mannooligosaccharides preparation as prebiotic
URI https://link.springer.com/article/10.1186/s40064-015-1565-7
https://www.ncbi.nlm.nih.gov/pubmed/26697281
https://www.proquest.com/docview/1749591658
https://www.proquest.com/docview/1751672255
https://www.proquest.com/docview/1868301556
https://pubmed.ncbi.nlm.nih.gov/PMC4678129
Volume 4
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