Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking
Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Nieter, Annabel [verfasserIn] |
|---|
| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Rechteinformationen: |
Nutzungsrecht: © Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved. |
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| Übergeordnetes Werk: |
Enthalten in: Food chemistry - Amsterdam [u.a.] : Elsevier, 1976, 209(2016), Seite 1-9 |
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| Übergeordnetes Werk: |
volume:209 ; year:2016 ; pages:1-9 |
| Links: |
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| DOI / URN: |
10.1016/j.foodchem.2016.03.106 |
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| 520 | |a Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. | ||
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10.1016/j.foodchem.2016.03.106 doi PQ20170301 (DE-627)OLC1981613234 (DE-599)GBVOLC1981613234 (PRQ)c1796-7cec3894ed248250c7f61e1bdaf3dd361ab86f87f80987df2a4ffb89290da4900 (KEY)0039580320160000209000000001heterologousproductionandcharacterizationofachloro DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Nieter, Annabel verfasserin aut Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. Nutzungsrecht: © Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved. Kelle, Sebastian oth Takenberg, Meike oth Linke, Diana oth Bunzel, Mirko oth Popper, Lutz oth Berger, Ralf G oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 209(2016), Seite 1-9 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:209 year:2016 pages:1-9 http://dx.doi.org/10.1016/j.foodchem.2016.03.106 Volltext http://www.sciencedirect.com/science/article/pii/S030881461630485X http://www.ncbi.nlm.nih.gov/pubmed/27173527 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 209 2016 1-9 |
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10.1016/j.foodchem.2016.03.106 doi PQ20170301 (DE-627)OLC1981613234 (DE-599)GBVOLC1981613234 (PRQ)c1796-7cec3894ed248250c7f61e1bdaf3dd361ab86f87f80987df2a4ffb89290da4900 (KEY)0039580320160000209000000001heterologousproductionandcharacterizationofachloro DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Nieter, Annabel verfasserin aut Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. Nutzungsrecht: © Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved. Kelle, Sebastian oth Takenberg, Meike oth Linke, Diana oth Bunzel, Mirko oth Popper, Lutz oth Berger, Ralf G oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 209(2016), Seite 1-9 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:209 year:2016 pages:1-9 http://dx.doi.org/10.1016/j.foodchem.2016.03.106 Volltext http://www.sciencedirect.com/science/article/pii/S030881461630485X http://www.ncbi.nlm.nih.gov/pubmed/27173527 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 209 2016 1-9 |
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10.1016/j.foodchem.2016.03.106 doi PQ20170301 (DE-627)OLC1981613234 (DE-599)GBVOLC1981613234 (PRQ)c1796-7cec3894ed248250c7f61e1bdaf3dd361ab86f87f80987df2a4ffb89290da4900 (KEY)0039580320160000209000000001heterologousproductionandcharacterizationofachloro DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Nieter, Annabel verfasserin aut Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. Nutzungsrecht: © Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved. Kelle, Sebastian oth Takenberg, Meike oth Linke, Diana oth Bunzel, Mirko oth Popper, Lutz oth Berger, Ralf G oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 209(2016), Seite 1-9 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:209 year:2016 pages:1-9 http://dx.doi.org/10.1016/j.foodchem.2016.03.106 Volltext http://www.sciencedirect.com/science/article/pii/S030881461630485X http://www.ncbi.nlm.nih.gov/pubmed/27173527 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 209 2016 1-9 |
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10.1016/j.foodchem.2016.03.106 doi PQ20170301 (DE-627)OLC1981613234 (DE-599)GBVOLC1981613234 (PRQ)c1796-7cec3894ed248250c7f61e1bdaf3dd361ab86f87f80987df2a4ffb89290da4900 (KEY)0039580320160000209000000001heterologousproductionandcharacterizationofachloro DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Nieter, Annabel verfasserin aut Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. Nutzungsrecht: © Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved. Kelle, Sebastian oth Takenberg, Meike oth Linke, Diana oth Bunzel, Mirko oth Popper, Lutz oth Berger, Ralf G oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 209(2016), Seite 1-9 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:209 year:2016 pages:1-9 http://dx.doi.org/10.1016/j.foodchem.2016.03.106 Volltext http://www.sciencedirect.com/science/article/pii/S030881461630485X http://www.ncbi.nlm.nih.gov/pubmed/27173527 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 209 2016 1-9 |
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10.1016/j.foodchem.2016.03.106 doi PQ20170301 (DE-627)OLC1981613234 (DE-599)GBVOLC1981613234 (PRQ)c1796-7cec3894ed248250c7f61e1bdaf3dd361ab86f87f80987df2a4ffb89290da4900 (KEY)0039580320160000209000000001heterologousproductionandcharacterizationofachloro DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Nieter, Annabel verfasserin aut Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. Nutzungsrecht: © Elsevier Ltd Copyright © 2016 Elsevier Ltd. All rights reserved. Kelle, Sebastian oth Takenberg, Meike oth Linke, Diana oth Bunzel, Mirko oth Popper, Lutz oth Berger, Ralf G oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 209(2016), Seite 1-9 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:209 year:2016 pages:1-9 http://dx.doi.org/10.1016/j.foodchem.2016.03.106 Volltext http://www.sciencedirect.com/science/article/pii/S030881461630485X http://www.ncbi.nlm.nih.gov/pubmed/27173527 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 209 2016 1-9 |
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heterologous production and characterization of a chlorogenic acid esterase from ustilago maydis with a potential use in baking |
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Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking |
| abstract |
Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. |
| abstractGer |
Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. |
| abstract_unstemmed |
Ustilago maydis, an edible mushroom growing on maize (Zea mays), is consumed as the food delicacy huitlacoche in Mexico. A chlorogenic acid esterase from this basidiomycete was expressed in good yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45.9UL(-1)). In contrast to previously described chlorogenic acid esterases, the reUmChlE was also active towards feruloylated saccharides. The enzyme preferred substrates with the ferulic acid esterified to the O-5 position of arabinose residues, typical of graminaceous monocots, over the O-2 position of arabinose or the O-6 position of galactose residues. Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid 18-fold more efficiently than methyl ferulate, p-coumarate or caffeate. Phenolic acids were released by reUmChlE from natural substrates, such as destarched wheat bran, sugar beet pectin and coffee pulp. Treatment of wheat dough using reUmChlE resulted in a noticeable softening indicating a potential application of the enzyme in bakery and confectionery. |
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Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking |
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http://dx.doi.org/10.1016/j.foodchem.2016.03.106 http://www.sciencedirect.com/science/article/pii/S030881461630485X http://www.ncbi.nlm.nih.gov/pubmed/27173527 |
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