Details
| Original language | English |
|---|---|
| Pages (from-to) | 1-9 |
| Number of pages | 9 |
| Journal | Food chemistry |
| Volume | 209 |
| Publication status | Published - 6 Apr 2016 |
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 5 L bioreactor scale (reUmChlE; 45.9 U L-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.
Keywords
- Baking, Basidiomycete, Chlorogenic acid, Coffee pulp, Esterase, Feruloylated saccharides, Heterologous expression, Pichia pastoris
ASJC Scopus subject areas
- Chemistry(all)
- Analytical Chemistry
- Agricultural and Biological Sciences(all)
- Food Science
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In: Food chemistry, Vol. 209, 06.04.2016, p. 1-9.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Heterologous production and characterization of a chlorogenic acid esterase from Ustilago maydis with a potential use in baking
AU - Nieter, Annabel
AU - Kelle, Sebastian
AU - Takenberg, Meike
AU - Linke, Diana
AU - Bunzel, Mirko
AU - Popper, Lutz
AU - Berger, Ralf G.
N1 - Funding information: Financial support of the work by the Federal Ministry of Education and Research cluster Biokatalyse2021 (P 37) is gratefully acknowledged. We thank Florian Paschen for performing the rheological measurements and Stefan Makollus for carrying out the baking trials as well as Rachel Schendel and Daniel Wefers for experimental support isolating feruloylated saccharides.
PY - 2016/4/6
Y1 - 2016/4/6
N2 - 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 5 L bioreactor scale (reUmChlE; 45.9 U L-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.
AB - 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 5 L bioreactor scale (reUmChlE; 45.9 U L-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.
KW - Baking
KW - Basidiomycete
KW - Chlorogenic acid
KW - Coffee pulp
KW - Esterase
KW - Feruloylated saccharides
KW - Heterologous expression
KW - Pichia pastoris
UR - http://www.scopus.com/inward/record.url?scp=84963642089&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2016.03.106
DO - 10.1016/j.foodchem.2016.03.106
M3 - Article
C2 - 27173527
AN - SCOPUS:84963642089
VL - 209
SP - 1
EP - 9
JO - Food chemistry
JF - Food chemistry
SN - 0308-8146
ER -