A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi
Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heter...
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Gespeichert in:
| Autor*in: |
Li, Jingjing [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media, LLC, part of Springer Nature 2020 |
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| Übergeordnetes Werk: |
Enthalten in: Applied biochemistry and biotechnology / A - Springer US, 1994, 192(2020), 4 vom: 28. Juli, Seite 1284-1297 |
|---|---|
| Übergeordnetes Werk: |
volume:192 ; year:2020 ; number:4 ; day:28 ; month:07 ; pages:1284-1297 |
| Links: |
|---|
| DOI / URN: |
10.1007/s12010-020-03368-w |
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OLC2120807760 |
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| 520 | |a Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. | ||
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10.1007/s12010-020-03368-w doi (DE-627)OLC2120807760 (DE-He213)s12010-020-03368-w-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Li, Jingjing verfasserin aut A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi 2020 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2020 Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. β-1,3(4)-glucanase Endo/exo-glucanase Fungus-growing termite Biochemical characterization Cao, Chunjing aut Jiang, Yutong aut Huang, Qihong aut Shen, Yulong aut Ni, Jinfeng (orcid)0000-0003-4743-292X aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 192(2020), 4 vom: 28. Juli, Seite 1284-1297 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:192 year:2020 number:4 day:28 month:07 pages:1284-1297 https://doi.org/10.1007/s12010-020-03368-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE 42.00 VZ AR 192 2020 4 28 07 1284-1297 |
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10.1007/s12010-020-03368-w doi (DE-627)OLC2120807760 (DE-He213)s12010-020-03368-w-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Li, Jingjing verfasserin aut A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi 2020 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2020 Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. β-1,3(4)-glucanase Endo/exo-glucanase Fungus-growing termite Biochemical characterization Cao, Chunjing aut Jiang, Yutong aut Huang, Qihong aut Shen, Yulong aut Ni, Jinfeng (orcid)0000-0003-4743-292X aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 192(2020), 4 vom: 28. Juli, Seite 1284-1297 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:192 year:2020 number:4 day:28 month:07 pages:1284-1297 https://doi.org/10.1007/s12010-020-03368-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE 42.00 VZ AR 192 2020 4 28 07 1284-1297 |
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10.1007/s12010-020-03368-w doi (DE-627)OLC2120807760 (DE-He213)s12010-020-03368-w-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Li, Jingjing verfasserin aut A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi 2020 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2020 Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. β-1,3(4)-glucanase Endo/exo-glucanase Fungus-growing termite Biochemical characterization Cao, Chunjing aut Jiang, Yutong aut Huang, Qihong aut Shen, Yulong aut Ni, Jinfeng (orcid)0000-0003-4743-292X aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 192(2020), 4 vom: 28. Juli, Seite 1284-1297 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:192 year:2020 number:4 day:28 month:07 pages:1284-1297 https://doi.org/10.1007/s12010-020-03368-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE 42.00 VZ AR 192 2020 4 28 07 1284-1297 |
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10.1007/s12010-020-03368-w doi (DE-627)OLC2120807760 (DE-He213)s12010-020-03368-w-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Li, Jingjing verfasserin aut A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi 2020 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2020 Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. β-1,3(4)-glucanase Endo/exo-glucanase Fungus-growing termite Biochemical characterization Cao, Chunjing aut Jiang, Yutong aut Huang, Qihong aut Shen, Yulong aut Ni, Jinfeng (orcid)0000-0003-4743-292X aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 192(2020), 4 vom: 28. Juli, Seite 1284-1297 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:192 year:2020 number:4 day:28 month:07 pages:1284-1297 https://doi.org/10.1007/s12010-020-03368-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE 42.00 VZ AR 192 2020 4 28 07 1284-1297 |
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10.1007/s12010-020-03368-w doi (DE-627)OLC2120807760 (DE-He213)s12010-020-03368-w-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Li, Jingjing verfasserin aut A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi 2020 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media, LLC, part of Springer Nature 2020 Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. β-1,3(4)-glucanase Endo/exo-glucanase Fungus-growing termite Biochemical characterization Cao, Chunjing aut Jiang, Yutong aut Huang, Qihong aut Shen, Yulong aut Ni, Jinfeng (orcid)0000-0003-4743-292X aut Enthalten in Applied biochemistry and biotechnology / A Springer US, 1994 192(2020), 4 vom: 28. Juli, Seite 1284-1297 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:192 year:2020 number:4 day:28 month:07 pages:1284-1297 https://doi.org/10.1007/s12010-020-03368-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE 42.00 VZ AR 192 2020 4 28 07 1284-1297 |
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A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi |
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A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi |
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Li, Jingjing |
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Li, Jingjing Cao, Chunjing Jiang, Yutong Huang, Qihong Shen, Yulong Ni, Jinfeng |
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a novel digestive gh16 β-1,3(4)-glucanase from the fungus-growing termite macrotermes barneyi |
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A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi |
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Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. © Springer Science+Business Media, LLC, part of Springer Nature 2020 |
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Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. © Springer Science+Business Media, LLC, part of Springer Nature 2020 |
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Abstract β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry. © Springer Science+Business Media, LLC, part of Springer Nature 2020 |
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A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi |
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