Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila

Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemic...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Bonzom, Cyrielle [verfasserIn] Hüttner, Silvia [verfasserIn] Mirgorodskaya, Ekaterina [verfasserIn] Chong, Sun-Li [verfasserIn] Uthoff, Stefan [verfasserIn] Steinbüchel, Alexander [verfasserIn] Verhaert, Raymond M. D. [verfasserIn] Olsson, Lisbeth [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	Mass spectrometry (MS) Enzyme activity Enzyme stability Heterologous production

Übergeordnetes Werk:	Enthalten in: AMB express - Heidelberg : Springer, 2011, 9(2019), 1 vom: 12. Aug.
Übergeordnetes Werk:	volume:9 ; year:2019 ; number:1 ; day:12 ; month:08

Links:	Volltext

DOI / URN:	10.1186/s13568-019-0852-z

Katalog-ID:	SPR03183695X

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520			\|a Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host.
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allfields	10.1186/s13568-019-0852-z doi (DE-627)SPR03183695X (SPR)s13568-019-0852-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Bonzom, Cyrielle verfasserin aut Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host. Mass spectrometry (MS) (dpeaa)DE-He213 Enzyme activity (dpeaa)DE-He213 Enzyme stability (dpeaa)DE-He213 Heterologous production (dpeaa)DE-He213 Hüttner, Silvia verfasserin aut Mirgorodskaya, Ekaterina verfasserin aut Chong, Sun-Li verfasserin aut Uthoff, Stefan verfasserin aut Steinbüchel, Alexander verfasserin aut Verhaert, Raymond M. D. verfasserin aut Olsson, Lisbeth verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 9(2019), 1 vom: 12. Aug. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:9 year:2019 number:1 day:12 month:08 https://dx.doi.org/10.1186/s13568-019-0852-z kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 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 58.30 ASE AR 9 2019 1 12 08
spelling	10.1186/s13568-019-0852-z doi (DE-627)SPR03183695X (SPR)s13568-019-0852-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Bonzom, Cyrielle verfasserin aut Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host. Mass spectrometry (MS) (dpeaa)DE-He213 Enzyme activity (dpeaa)DE-He213 Enzyme stability (dpeaa)DE-He213 Heterologous production (dpeaa)DE-He213 Hüttner, Silvia verfasserin aut Mirgorodskaya, Ekaterina verfasserin aut Chong, Sun-Li verfasserin aut Uthoff, Stefan verfasserin aut Steinbüchel, Alexander verfasserin aut Verhaert, Raymond M. D. verfasserin aut Olsson, Lisbeth verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 9(2019), 1 vom: 12. Aug. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:9 year:2019 number:1 day:12 month:08 https://dx.doi.org/10.1186/s13568-019-0852-z kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 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 58.30 ASE AR 9 2019 1 12 08
allfields_unstemmed	10.1186/s13568-019-0852-z doi (DE-627)SPR03183695X (SPR)s13568-019-0852-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Bonzom, Cyrielle verfasserin aut Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host. Mass spectrometry (MS) (dpeaa)DE-He213 Enzyme activity (dpeaa)DE-He213 Enzyme stability (dpeaa)DE-He213 Heterologous production (dpeaa)DE-He213 Hüttner, Silvia verfasserin aut Mirgorodskaya, Ekaterina verfasserin aut Chong, Sun-Li verfasserin aut Uthoff, Stefan verfasserin aut Steinbüchel, Alexander verfasserin aut Verhaert, Raymond M. D. verfasserin aut Olsson, Lisbeth verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 9(2019), 1 vom: 12. Aug. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:9 year:2019 number:1 day:12 month:08 https://dx.doi.org/10.1186/s13568-019-0852-z kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 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 58.30 ASE AR 9 2019 1 12 08
allfieldsGer	10.1186/s13568-019-0852-z doi (DE-627)SPR03183695X (SPR)s13568-019-0852-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Bonzom, Cyrielle verfasserin aut Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host. Mass spectrometry (MS) (dpeaa)DE-He213 Enzyme activity (dpeaa)DE-He213 Enzyme stability (dpeaa)DE-He213 Heterologous production (dpeaa)DE-He213 Hüttner, Silvia verfasserin aut Mirgorodskaya, Ekaterina verfasserin aut Chong, Sun-Li verfasserin aut Uthoff, Stefan verfasserin aut Steinbüchel, Alexander verfasserin aut Verhaert, Raymond M. D. verfasserin aut Olsson, Lisbeth verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 9(2019), 1 vom: 12. Aug. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:9 year:2019 number:1 day:12 month:08 https://dx.doi.org/10.1186/s13568-019-0852-z kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 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 58.30 ASE AR 9 2019 1 12 08
allfieldsSound	10.1186/s13568-019-0852-z doi (DE-627)SPR03183695X (SPR)s13568-019-0852-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Bonzom, Cyrielle verfasserin aut Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host. Mass spectrometry (MS) (dpeaa)DE-He213 Enzyme activity (dpeaa)DE-He213 Enzyme stability (dpeaa)DE-He213 Heterologous production (dpeaa)DE-He213 Hüttner, Silvia verfasserin aut Mirgorodskaya, Ekaterina verfasserin aut Chong, Sun-Li verfasserin aut Uthoff, Stefan verfasserin aut Steinbüchel, Alexander verfasserin aut Verhaert, Raymond M. D. verfasserin aut Olsson, Lisbeth verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 9(2019), 1 vom: 12. Aug. (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:9 year:2019 number:1 day:12 month:08 https://dx.doi.org/10.1186/s13568-019-0852-z kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 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 58.30 ASE AR 9 2019 1 12 08
language	English
source	Enthalten in AMB express 9(2019), 1 vom: 12. Aug. volume:9 year:2019 number:1 day:12 month:08
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topic_facet	Mass spectrometry (MS) Enzyme activity Enzyme stability Heterologous production
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author	Bonzom, Cyrielle
spellingShingle	Bonzom, Cyrielle ddc 570 bkl 58.30 misc Mass spectrometry (MS) misc Enzyme activity misc Enzyme stability misc Heterologous production Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila
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topic_title	570 ASE 58.30 bkl Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila Mass spectrometry (MS) (dpeaa)DE-He213 Enzyme activity (dpeaa)DE-He213 Enzyme stability (dpeaa)DE-He213 Heterologous production (dpeaa)DE-He213
topic	ddc 570 bkl 58.30 misc Mass spectrometry (MS) misc Enzyme activity misc Enzyme stability misc Heterologous production
topic_unstemmed	ddc 570 bkl 58.30 misc Mass spectrometry (MS) misc Enzyme activity misc Enzyme stability misc Heterologous production
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title	Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila
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title_full	Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila
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author_browse	Bonzom, Cyrielle Hüttner, Silvia Mirgorodskaya, Ekaterina Chong, Sun-Li Uthoff, Stefan Steinbüchel, Alexander Verhaert, Raymond M. D. Olsson, Lisbeth
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title_sort	glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from myceliophthora thermophila
title_auth	Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila
abstract	Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host.
abstractGer	Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host.
abstract_unstemmed	Abstract Heterologous protein production is widely used in industrial biotechnology. However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. We conclude that the biotechnological value of an enzyme can be optimized for a specific application by carefully selecting the production host.
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title_short	Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila
url	https://dx.doi.org/10.1186/s13568-019-0852-z
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author2	Hüttner, Silvia Mirgorodskaya, Ekaterina Chong, Sun-Li Uthoff, Stefan Steinbüchel, Alexander Verhaert, Raymond M. D. Olsson, Lisbeth
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up_date	2024-07-04T01:27:33.036Z
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However, using non-native production hosts can lead to enzymes with altered post-translational modifications, such as glycosylation. We have investigated how production in a non-native host affects the physicochemical properties and enzymatic activity of a feruloyl esterase from Myceliophthora thermophila, MtFae1a. The enzyme was produced in two microorganisms that introduce glycosylation (M. thermophila and Pichia pastoris) and in Escherichia coli (non-glycosylated). Mass spectrometric analysis confirmed the presence of glycosylation and revealed differences in the lengths of glycan chains between the enzymes produced in M. thermophila and P. pastoris. The melting temperature and the optimal temperature for activity of the non-glycosylated enzyme were considerably lower than those of the glycosylated enzymes. The three MtFae1a versions also exhibited differences in specific activity and specificity. The catalytic efficiency of the glycosylated enzymes were more than 10 times higher than that of the non-glycosylated one. In biotechnology, immobilization is often used to allow reusing enzyme and was investigated on mesoporous silica particles. We found the binding kinetics and immobilization yield differed between the enzyme versions. The largest differences were observed when comparing enzymes with and without glycosylation, but significant variations were also observed between the two differently glycosylated enzymes. 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Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila

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