Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)

Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type st...
Ausführliche Beschreibung

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Autor*in:	Qiu, Yibin [verfasserIn] Zhu, Yifan Zhan, Yijing Zhang, Yatao Sha, Yuanyuan Xu, Zongqi Li, Sha Feng, Xiaohai Xu, Hong

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	Inulin hydrolase Poly-(γ-glutamic acid) Jerusalem artichoke biorefinery

Anmerkung:	© The Author(s) 2019

Übergeordnetes Werk:	Enthalten in: Biotechnology for biofuels - London : BioMed Central, 2008, 12(2019), 1 vom: 13. Juni
Übergeordnetes Werk:	volume:12 ; year:2019 ; number:1 ; day:13 ; month:06

Links:	Volltext

DOI / URN:	10.1186/s13068-019-1485-9

Katalog-ID:	SPR030160332

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520			\|a Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery.
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matchkey_str	article:17546834:2019----::ytmtcnaelnotenlnyrlsfobcluayoiufcesoefcetov
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allfields	10.1186/s13068-019-1485-9 doi (DE-627)SPR030160332 (SPR)s13068-019-1485-9-e DE-627 ger DE-627 rakwb eng Qiu, Yibin verfasserin aut Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid) 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. Inulin hydrolase (dpeaa)DE-He213 Poly-(γ-glutamic acid) (dpeaa)DE-He213 Jerusalem artichoke biorefinery (dpeaa)DE-He213 Zhu, Yifan aut Zhan, Yijing aut Zhang, Yatao aut Sha, Yuanyuan aut Zhan, Yijing aut Xu, Zongqi aut Li, Sha aut Feng, Xiaohai aut Xu, Hong (orcid)0000-0003-0601-6321 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 13. Juni (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:13 month:06 https://dx.doi.org/10.1186/s13068-019-1485-9 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 13 06
spelling	10.1186/s13068-019-1485-9 doi (DE-627)SPR030160332 (SPR)s13068-019-1485-9-e DE-627 ger DE-627 rakwb eng Qiu, Yibin verfasserin aut Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid) 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. Inulin hydrolase (dpeaa)DE-He213 Poly-(γ-glutamic acid) (dpeaa)DE-He213 Jerusalem artichoke biorefinery (dpeaa)DE-He213 Zhu, Yifan aut Zhan, Yijing aut Zhang, Yatao aut Sha, Yuanyuan aut Zhan, Yijing aut Xu, Zongqi aut Li, Sha aut Feng, Xiaohai aut Xu, Hong (orcid)0000-0003-0601-6321 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 13. Juni (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:13 month:06 https://dx.doi.org/10.1186/s13068-019-1485-9 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 13 06
allfields_unstemmed	10.1186/s13068-019-1485-9 doi (DE-627)SPR030160332 (SPR)s13068-019-1485-9-e DE-627 ger DE-627 rakwb eng Qiu, Yibin verfasserin aut Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid) 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. Inulin hydrolase (dpeaa)DE-He213 Poly-(γ-glutamic acid) (dpeaa)DE-He213 Jerusalem artichoke biorefinery (dpeaa)DE-He213 Zhu, Yifan aut Zhan, Yijing aut Zhang, Yatao aut Sha, Yuanyuan aut Zhan, Yijing aut Xu, Zongqi aut Li, Sha aut Feng, Xiaohai aut Xu, Hong (orcid)0000-0003-0601-6321 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 13. Juni (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:13 month:06 https://dx.doi.org/10.1186/s13068-019-1485-9 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 13 06
allfieldsGer	10.1186/s13068-019-1485-9 doi (DE-627)SPR030160332 (SPR)s13068-019-1485-9-e DE-627 ger DE-627 rakwb eng Qiu, Yibin verfasserin aut Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid) 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. Inulin hydrolase (dpeaa)DE-He213 Poly-(γ-glutamic acid) (dpeaa)DE-He213 Jerusalem artichoke biorefinery (dpeaa)DE-He213 Zhu, Yifan aut Zhan, Yijing aut Zhang, Yatao aut Sha, Yuanyuan aut Zhan, Yijing aut Xu, Zongqi aut Li, Sha aut Feng, Xiaohai aut Xu, Hong (orcid)0000-0003-0601-6321 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 13. Juni (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:13 month:06 https://dx.doi.org/10.1186/s13068-019-1485-9 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 13 06
allfieldsSound	10.1186/s13068-019-1485-9 doi (DE-627)SPR030160332 (SPR)s13068-019-1485-9-e DE-627 ger DE-627 rakwb eng Qiu, Yibin verfasserin aut Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid) 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. Inulin hydrolase (dpeaa)DE-He213 Poly-(γ-glutamic acid) (dpeaa)DE-He213 Jerusalem artichoke biorefinery (dpeaa)DE-He213 Zhu, Yifan aut Zhan, Yijing aut Zhang, Yatao aut Sha, Yuanyuan aut Zhan, Yijing aut Xu, Zongqi aut Li, Sha aut Feng, Xiaohai aut Xu, Hong (orcid)0000-0003-0601-6321 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 13. Juni (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:13 month:06 https://dx.doi.org/10.1186/s13068-019-1485-9 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 13 06
language	English
source	Enthalten in Biotechnology for biofuels 12(2019), 1 vom: 13. Juni volume:12 year:2019 number:1 day:13 month:06
sourceStr	Enthalten in Biotechnology for biofuels 12(2019), 1 vom: 13. Juni volume:12 year:2019 number:1 day:13 month:06
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topic_facet	Inulin hydrolase Poly-(γ-glutamic acid) Jerusalem artichoke biorefinery
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authorswithroles_txt_mv	Qiu, Yibin @@aut@@ Zhu, Yifan @@aut@@ Zhan, Yijing @@aut@@ Zhang, Yatao @@aut@@ Sha, Yuanyuan @@aut@@ Xu, Zongqi @@aut@@ Li, Sha @@aut@@ Feng, Xiaohai @@aut@@ Xu, Hong @@aut@@
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author	Qiu, Yibin
spellingShingle	Qiu, Yibin misc Inulin hydrolase misc Poly-(γ-glutamic acid) misc Jerusalem artichoke biorefinery Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)
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topic_title	Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid) Inulin hydrolase (dpeaa)DE-He213 Poly-(γ-glutamic acid) (dpeaa)DE-He213 Jerusalem artichoke biorefinery (dpeaa)DE-He213
topic	misc Inulin hydrolase misc Poly-(γ-glutamic acid) misc Jerusalem artichoke biorefinery
topic_unstemmed	misc Inulin hydrolase misc Poly-(γ-glutamic acid) misc Jerusalem artichoke biorefinery
topic_browse	misc Inulin hydrolase misc Poly-(γ-glutamic acid) misc Jerusalem artichoke biorefinery
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title	Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)
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title_full	Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)
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author_browse	Qiu, Yibin Zhu, Yifan Zhan, Yijing Zhang, Yatao Sha, Yuanyuan Xu, Zongqi Li, Sha Feng, Xiaohai Xu, Hong
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title_sort	systematic unravelling of the inulin hydrolase from bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)
title_auth	Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)
abstract	Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. © The Author(s) 2019
abstractGer	Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. © The Author(s) 2019
abstract_unstemmed	Background Bacillus amyloliquefaciens NB is a newly discovered strain, which produces poly-(γ-glutamic acid) (γ-PGA) from raw extracted inulin of Jerusalem artichoke tubers; however, the underlying mechanisms remain unknown. To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. Conclusions The inulin hydrolase CscA is critical for inulin metabolism in B. amyloliquefaciens and indicates potential application in Jerusalem artichoke biorefinery. © The Author(s) 2019
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title_short	Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)
url	https://dx.doi.org/10.1186/s13068-019-1485-9
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author2	Zhu, Yifan Zhan, Yijing Zhang, Yatao Sha, Yuanyuan Xu, Zongqi Li, Sha Feng, Xiaohai Xu, Hong
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To address this problem, we identified the inulin hydrolase in wild-type strain B. amyloliquefaciens NB. Results The novel inulin hydrolase (CscA) was discovered from strain NB, with high inulinase activity (987.0 U/mg at 55 °C) and strong resistance at pH values between 8.0 and 11.0, suggesting the potential application of CscA in Jerusalem artichoke biorefinery. CscA exhibited a kcat/Km of (6.93 ± 0.27) × $ 10^{3} $ for inulin; its enzymatic activity was stimulated by metal ions, like $ K^{+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Similar to their role in glycoside hydrolase 32 family enzymes, the conserved Asp37, Asp161, and Glu215 residues of CscA contribute to its catalytic activity. Targeted disruption of CscA gene suppressed inulin utilization by strain NB. Overexpression of CscA significantly enhanced the γ-PGA generation by 19.2% through enhancement in inulin consumption. 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Systematic unravelling of the inulin hydrolase from Bacillus amyloliquefaciens for efficient conversion of inulin to poly-(γ-glutamic acid)

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