Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach

Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first...
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Autor*in:	Kong, Jing [verfasserIn] Miao, Lin Lu, Zhihui Wang, Shuhui Zhao, Baixiang Zhang, Cuiying Xiao, Dongguang Teo, Desmond Leong, Susanna Su Jan Wong, Adison Yu, Aiqun

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	Triterpenoid Amyrin Metabolic engineering Protein engineering

Anmerkung:	© The Author(s) 2022

Übergeordnetes Werk:	Enthalten in: Microbial cell factories - London : Biomed Central, 2002, 21(2022), 1 vom: 09. Sept.
Übergeordnetes Werk:	volume:21 ; year:2022 ; number:1 ; day:09 ; month:09

Links:	Volltext

DOI / URN:	10.1186/s12934-022-01915-0

Katalog-ID:	SPR050981137

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520			\|a Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica.
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allfields	10.1186/s12934-022-01915-0 doi (DE-627)SPR050981137 (SPR)s12934-022-01915-0-e DE-627 ger DE-627 rakwb eng Kong, Jing verfasserin aut Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. Triterpenoid (dpeaa)DE-He213 Amyrin (dpeaa)DE-He213 Metabolic engineering (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Miao, Lin aut Lu, Zhihui aut Wang, Shuhui aut Zhao, Baixiang aut Zhang, Cuiying aut Xiao, Dongguang aut Teo, Desmond aut Leong, Susanna Su Jan aut Wong, Adison aut Yu, Aiqun aut Enthalten in Microbial cell factories London : Biomed Central, 2002 21(2022), 1 vom: 09. Sept. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:21 year:2022 number:1 day:09 month:09 https://dx.doi.org/10.1186/s12934-022-01915-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_224 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_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 21 2022 1 09 09
spelling	10.1186/s12934-022-01915-0 doi (DE-627)SPR050981137 (SPR)s12934-022-01915-0-e DE-627 ger DE-627 rakwb eng Kong, Jing verfasserin aut Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. Triterpenoid (dpeaa)DE-He213 Amyrin (dpeaa)DE-He213 Metabolic engineering (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Miao, Lin aut Lu, Zhihui aut Wang, Shuhui aut Zhao, Baixiang aut Zhang, Cuiying aut Xiao, Dongguang aut Teo, Desmond aut Leong, Susanna Su Jan aut Wong, Adison aut Yu, Aiqun aut Enthalten in Microbial cell factories London : Biomed Central, 2002 21(2022), 1 vom: 09. Sept. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:21 year:2022 number:1 day:09 month:09 https://dx.doi.org/10.1186/s12934-022-01915-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_224 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_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 21 2022 1 09 09
allfields_unstemmed	10.1186/s12934-022-01915-0 doi (DE-627)SPR050981137 (SPR)s12934-022-01915-0-e DE-627 ger DE-627 rakwb eng Kong, Jing verfasserin aut Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. Triterpenoid (dpeaa)DE-He213 Amyrin (dpeaa)DE-He213 Metabolic engineering (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Miao, Lin aut Lu, Zhihui aut Wang, Shuhui aut Zhao, Baixiang aut Zhang, Cuiying aut Xiao, Dongguang aut Teo, Desmond aut Leong, Susanna Su Jan aut Wong, Adison aut Yu, Aiqun aut Enthalten in Microbial cell factories London : Biomed Central, 2002 21(2022), 1 vom: 09. Sept. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:21 year:2022 number:1 day:09 month:09 https://dx.doi.org/10.1186/s12934-022-01915-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_224 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_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 21 2022 1 09 09
allfieldsGer	10.1186/s12934-022-01915-0 doi (DE-627)SPR050981137 (SPR)s12934-022-01915-0-e DE-627 ger DE-627 rakwb eng Kong, Jing verfasserin aut Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. Triterpenoid (dpeaa)DE-He213 Amyrin (dpeaa)DE-He213 Metabolic engineering (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Miao, Lin aut Lu, Zhihui aut Wang, Shuhui aut Zhao, Baixiang aut Zhang, Cuiying aut Xiao, Dongguang aut Teo, Desmond aut Leong, Susanna Su Jan aut Wong, Adison aut Yu, Aiqun aut Enthalten in Microbial cell factories London : Biomed Central, 2002 21(2022), 1 vom: 09. Sept. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:21 year:2022 number:1 day:09 month:09 https://dx.doi.org/10.1186/s12934-022-01915-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_224 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_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 21 2022 1 09 09
allfieldsSound	10.1186/s12934-022-01915-0 doi (DE-627)SPR050981137 (SPR)s12934-022-01915-0-e DE-627 ger DE-627 rakwb eng Kong, Jing verfasserin aut Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. Triterpenoid (dpeaa)DE-He213 Amyrin (dpeaa)DE-He213 Metabolic engineering (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Miao, Lin aut Lu, Zhihui aut Wang, Shuhui aut Zhao, Baixiang aut Zhang, Cuiying aut Xiao, Dongguang aut Teo, Desmond aut Leong, Susanna Su Jan aut Wong, Adison aut Yu, Aiqun aut Enthalten in Microbial cell factories London : Biomed Central, 2002 21(2022), 1 vom: 09. Sept. (DE-627)355987651 (DE-600)2091377-1 1475-2859 nnns volume:21 year:2022 number:1 day:09 month:09 https://dx.doi.org/10.1186/s12934-022-01915-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_224 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_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 21 2022 1 09 09
language	English
source	Enthalten in Microbial cell factories 21(2022), 1 vom: 09. Sept. volume:21 year:2022 number:1 day:09 month:09
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topic_facet	Triterpenoid Amyrin Metabolic engineering Protein engineering
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authorswithroles_txt_mv	Kong, Jing @@aut@@ Miao, Lin @@aut@@ Lu, Zhihui @@aut@@ Wang, Shuhui @@aut@@ Zhao, Baixiang @@aut@@ Zhang, Cuiying @@aut@@ Xiao, Dongguang @@aut@@ Teo, Desmond @@aut@@ Leong, Susanna Su Jan @@aut@@ Wong, Adison @@aut@@ Yu, Aiqun @@aut@@
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In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. 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author	Kong, Jing
spellingShingle	Kong, Jing misc Triterpenoid misc Amyrin misc Metabolic engineering misc Protein engineering Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach
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topic_title	Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach Triterpenoid (dpeaa)DE-He213 Amyrin (dpeaa)DE-He213 Metabolic engineering (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213
topic	misc Triterpenoid misc Amyrin misc Metabolic engineering misc Protein engineering
topic_unstemmed	misc Triterpenoid misc Amyrin misc Metabolic engineering misc Protein engineering
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title	Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach
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title_full	Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach
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author_browse	Kong, Jing Miao, Lin Lu, Zhihui Wang, Shuhui Zhao, Baixiang Zhang, Cuiying Xiao, Dongguang Teo, Desmond Leong, Susanna Su Jan Wong, Adison Yu, Aiqun
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title_sort	enhanced production of amyrin in yarrowia lipolytica using a combinatorial protein and metabolic engineering approach
title_auth	Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach
abstract	Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. © The Author(s) 2022
abstractGer	Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. © The Author(s) 2022
abstract_unstemmed	Background Amyrin is an important triterpenoid and precursor to a wide range of cosmetic, pharmaceutical and nutraceutical products. In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. Conclusions The design workflow demonstrated herein is simple and remarkably effective in amplifying triterpenoid biosynthesis in the yeast Y. lipolytica. © The Author(s) 2022
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title_short	Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach
url	https://dx.doi.org/10.1186/s12934-022-01915-0
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author2	Miao, Lin Lu, Zhihui Wang, Shuhui Zhao, Baixiang Zhang, Cuiying Xiao, Dongguang Teo, Desmond Leong, Susanna Su Jan Wong, Adison Yu, Aiqun
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up_date	2024-07-03T19:01:45.149Z
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In this study, we metabolically engineered the oleaginous yeast, Yarrowia lipolytica to produce α- and β-amyrin on simple sugar and waste cooking oil. Results We first validated the in vivo enzymatic activity of a multi-functional amyrin synthase (CrMAS) from Catharanthus roseus, by expressing its codon-optimized gene in Y. lipolytica and assayed for amyrins. To increase yield, prevailing genes in the mevalonate pathway, namely HMG1, ERG20, ERG9 and ERG1, were overexpressed singly and in combination to direct flux towards amyrin biosynthesis. By means of a semi-rational protein engineering approach, we augmented the catalytic activity of CrMAS and attained ~ 10-folds higher production level on glucose. When applied together, protein engineering with enhanced precursor supplies resulted in more than 20-folds increase in total amyrins. We also investigated the effects of different fermentation conditions in flask cultures, including temperature, volumetric oxygen mass transfer coefficient and carbon source types. The optimized fermentation condition attained titers of at least 100 mg/L α-amyrin and 20 mg/L β-amyrin. 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Enhanced production of amyrin in Yarrowia lipolytica using a combinatorial protein and metabolic engineering approach

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