Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production

Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< w...
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Autor*in:	Zewang Guo [verfasserIn] Denghui Chen [verfasserIn] Qi Xiong [verfasserIn] Miao Liang [verfasserIn] Pengfei Li [verfasserIn] Zehui Gong [verfasserIn] Junzhi Qiu [verfasserIn] Liaoyuan Zhang [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	leucine dehydrogenase L- trimethylpyruvate reductive amination whole-cell biocatalysis

Übergeordnetes Werk:	In: Catalysts - MDPI AG, 2012, 12(2022), 9, p 971
Übergeordnetes Werk:	volume:12 ; year:2022 ; number:9, p 971

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/catal12090971

Katalog-ID:	DOAJ087032309

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allfields	10.3390/catal12090971 doi (DE-627)DOAJ087032309 (DE-599)DOAJa025585997d541ada11fa7ab82a4bf04 DE-627 ger DE-627 rakwb eng TP1-1185 QD1-999 Zewang Guo verfasserin aut Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production. leucine dehydrogenase L-<i<tert</i<-leucine trimethylpyruvate reductive amination whole-cell biocatalysis Chemical technology Chemistry Denghui Chen verfasserin aut Qi Xiong verfasserin aut Miao Liang verfasserin aut Pengfei Li verfasserin aut Zehui Gong verfasserin aut Junzhi Qiu verfasserin aut Liaoyuan Zhang verfasserin aut In Catalysts MDPI AG, 2012 12(2022), 9, p 971 (DE-627)71862646X (DE-600)2662126-5 20734344 nnns volume:12 year:2022 number:9, p 971 https://doi.org/10.3390/catal12090971 kostenfrei https://doaj.org/article/a025585997d541ada11fa7ab82a4bf04 kostenfrei https://www.mdpi.com/2073-4344/12/9/971 kostenfrei https://doaj.org/toc/2073-4344 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 9, p 971
spelling	10.3390/catal12090971 doi (DE-627)DOAJ087032309 (DE-599)DOAJa025585997d541ada11fa7ab82a4bf04 DE-627 ger DE-627 rakwb eng TP1-1185 QD1-999 Zewang Guo verfasserin aut Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production. leucine dehydrogenase L-<i<tert</i<-leucine trimethylpyruvate reductive amination whole-cell biocatalysis Chemical technology Chemistry Denghui Chen verfasserin aut Qi Xiong verfasserin aut Miao Liang verfasserin aut Pengfei Li verfasserin aut Zehui Gong verfasserin aut Junzhi Qiu verfasserin aut Liaoyuan Zhang verfasserin aut In Catalysts MDPI AG, 2012 12(2022), 9, p 971 (DE-627)71862646X (DE-600)2662126-5 20734344 nnns volume:12 year:2022 number:9, p 971 https://doi.org/10.3390/catal12090971 kostenfrei https://doaj.org/article/a025585997d541ada11fa7ab82a4bf04 kostenfrei https://www.mdpi.com/2073-4344/12/9/971 kostenfrei https://doaj.org/toc/2073-4344 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 9, p 971
allfields_unstemmed	10.3390/catal12090971 doi (DE-627)DOAJ087032309 (DE-599)DOAJa025585997d541ada11fa7ab82a4bf04 DE-627 ger DE-627 rakwb eng TP1-1185 QD1-999 Zewang Guo verfasserin aut Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production. leucine dehydrogenase L-<i<tert</i<-leucine trimethylpyruvate reductive amination whole-cell biocatalysis Chemical technology Chemistry Denghui Chen verfasserin aut Qi Xiong verfasserin aut Miao Liang verfasserin aut Pengfei Li verfasserin aut Zehui Gong verfasserin aut Junzhi Qiu verfasserin aut Liaoyuan Zhang verfasserin aut In Catalysts MDPI AG, 2012 12(2022), 9, p 971 (DE-627)71862646X (DE-600)2662126-5 20734344 nnns volume:12 year:2022 number:9, p 971 https://doi.org/10.3390/catal12090971 kostenfrei https://doaj.org/article/a025585997d541ada11fa7ab82a4bf04 kostenfrei https://www.mdpi.com/2073-4344/12/9/971 kostenfrei https://doaj.org/toc/2073-4344 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 9, p 971
allfieldsGer	10.3390/catal12090971 doi (DE-627)DOAJ087032309 (DE-599)DOAJa025585997d541ada11fa7ab82a4bf04 DE-627 ger DE-627 rakwb eng TP1-1185 QD1-999 Zewang Guo verfasserin aut Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production. leucine dehydrogenase L-<i<tert</i<-leucine trimethylpyruvate reductive amination whole-cell biocatalysis Chemical technology Chemistry Denghui Chen verfasserin aut Qi Xiong verfasserin aut Miao Liang verfasserin aut Pengfei Li verfasserin aut Zehui Gong verfasserin aut Junzhi Qiu verfasserin aut Liaoyuan Zhang verfasserin aut In Catalysts MDPI AG, 2012 12(2022), 9, p 971 (DE-627)71862646X (DE-600)2662126-5 20734344 nnns volume:12 year:2022 number:9, p 971 https://doi.org/10.3390/catal12090971 kostenfrei https://doaj.org/article/a025585997d541ada11fa7ab82a4bf04 kostenfrei https://www.mdpi.com/2073-4344/12/9/971 kostenfrei https://doaj.org/toc/2073-4344 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 9, p 971
allfieldsSound	10.3390/catal12090971 doi (DE-627)DOAJ087032309 (DE-599)DOAJa025585997d541ada11fa7ab82a4bf04 DE-627 ger DE-627 rakwb eng TP1-1185 QD1-999 Zewang Guo verfasserin aut Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production. leucine dehydrogenase L-<i<tert</i<-leucine trimethylpyruvate reductive amination whole-cell biocatalysis Chemical technology Chemistry Denghui Chen verfasserin aut Qi Xiong verfasserin aut Miao Liang verfasserin aut Pengfei Li verfasserin aut Zehui Gong verfasserin aut Junzhi Qiu verfasserin aut Liaoyuan Zhang verfasserin aut In Catalysts MDPI AG, 2012 12(2022), 9, p 971 (DE-627)71862646X (DE-600)2662126-5 20734344 nnns volume:12 year:2022 number:9, p 971 https://doi.org/10.3390/catal12090971 kostenfrei https://doaj.org/article/a025585997d541ada11fa7ab82a4bf04 kostenfrei https://www.mdpi.com/2073-4344/12/9/971 kostenfrei https://doaj.org/toc/2073-4344 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 9, p 971
language	English
source	In Catalysts 12(2022), 9, p 971 volume:12 year:2022 number:9, p 971
sourceStr	In Catalysts 12(2022), 9, p 971 volume:12 year:2022 number:9, p 971
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	leucine dehydrogenase L-<i<tert</i<-leucine trimethylpyruvate reductive amination whole-cell biocatalysis Chemical technology Chemistry
isfreeaccess_bool	true
container_title	Catalysts
authorswithroles_txt_mv	Zewang Guo @@aut@@ Denghui Chen @@aut@@ Qi Xiong @@aut@@ Miao Liang @@aut@@ Pengfei Li @@aut@@ Zehui Gong @@aut@@ Junzhi Qiu @@aut@@ Liaoyuan Zhang @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	71862646X
id	DOAJ087032309
language_de	englisch
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callnumber-first	T - Technology
author	Zewang Guo
spellingShingle	Zewang Guo misc TP1-1185 misc QD1-999 misc leucine dehydrogenase misc L-<i<tert</i<-leucine misc trimethylpyruvate misc reductive amination misc whole-cell biocatalysis misc Chemical technology misc Chemistry Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production
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topic_title	TP1-1185 QD1-999 Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production leucine dehydrogenase L-<i<tert</i<-leucine trimethylpyruvate reductive amination whole-cell biocatalysis
topic	misc TP1-1185 misc QD1-999 misc leucine dehydrogenase misc L-<i<tert</i<-leucine misc trimethylpyruvate misc reductive amination misc whole-cell biocatalysis misc Chemical technology misc Chemistry
topic_unstemmed	misc TP1-1185 misc QD1-999 misc leucine dehydrogenase misc L-<i<tert</i<-leucine misc trimethylpyruvate misc reductive amination misc whole-cell biocatalysis misc Chemical technology misc Chemistry
topic_browse	misc TP1-1185 misc QD1-999 misc leucine dehydrogenase misc L-<i<tert</i<-leucine misc trimethylpyruvate misc reductive amination misc whole-cell biocatalysis misc Chemical technology misc Chemistry
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title	Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production
ctrlnum	(DE-627)DOAJ087032309 (DE-599)DOAJa025585997d541ada11fa7ab82a4bf04
title_full	Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production
author_sort	Zewang Guo
journal	Catalysts
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author_browse	Zewang Guo Denghui Chen Qi Xiong Miao Liang Pengfei Li Zehui Gong Junzhi Qiu Liaoyuan Zhang
container_volume	12
class	TP1-1185 QD1-999
format_se	Elektronische Aufsätze
author-letter	Zewang Guo
doi_str_mv	10.3390/catal12090971
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title_sort	characterization of a new marine leucine dehydrogenase from <i<pseudomonas balearica</i< and its application for l-<i<tert</i<-leucine production
callnumber	TP1-1185
title_auth	Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production
abstract	Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production.
abstractGer	Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production.
abstract_unstemmed	Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-<i<tert</i<-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named <i<Pb</i<LeuDH from marine <i<Pseudomonas balearica</i< was heterologously over-expressed in <i<Escherichia coli</i<, followed by purification and characterization. <i<Pb</i<LeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and <i<α</i<-keto acids. Notably, compared with those reported LeuDHs, <i<Pb</i<LeuDH exhibited excellent catalytic efficiency for TMP with a <i<K</i<<sub<m</sub< value of 4.92 mM and a <i<k</i<<sub<cat</sub</<i<K</i<<sub<m</sub< value of 24.49 s<sup<−1</sup< mM<sup<−1</sup<. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant <i<E. coli</i< as a catalyst, which co-expressed <i<Pb</i<LeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L<sup<−1</sup<) L-Tle was achieved with a 96.1% yield and 2.39 g L<sup<−1</sup< h<sup<−1</sup< productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production.
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container_issue	9, p 971
title_short	Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production
url	https://doi.org/10.3390/catal12090971 https://doaj.org/article/a025585997d541ada11fa7ab82a4bf04 https://www.mdpi.com/2073-4344/12/9/971 https://doaj.org/toc/2073-4344
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author2	Denghui Chen Qi Xiong Miao Liang Pengfei Li Zehui Gong Junzhi Qiu Liaoyuan Zhang
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up_date	2024-07-03T23:57:02.116Z
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Characterization of a New Marine Leucine Dehydrogenase from <i<Pseudomonas balearica</i< and Its Application for L-<i<tert</i<-Leucine Production

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