A p-coumaroyl esterase from Rhizoctonia solani with a pronounced chlorogenic acid esterase activity

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Authors

  • Annabel Nieter
  • Sebastian Kelle
  • Diana Linke
  • Ralf G. Berger

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Original languageEnglish
Pages (from-to)153-161
Number of pages9
JournalNew biotechnology
Volume37
Publication statusPublished - 31 Jan 2017

Abstract

Extracellular esterase activity was detected in submerged cultures of Rhizoctonia solani grown in the presence of sugar beet pectin or Tween 80. Putative type B feruloyl esterase (FAE) coding sequences found in the genome data of the basidiomycete were heterologously expressed in Pichia pastoris. Recombinant enzyme production on the 5-L bioreactor scale (Rs pCAE: 3245 U L−1) exceeded the productivity of the wild type strain by a factor of 800. Based on substrate specificity profiling, the purified recombinant Rs pCAE was classified as a p-coumaroyl esterase (pCAE) with a pronounced chlorogenic acid esterase side activity. The Rs pCAE was also active on methyl cinnamate, caffeate and ferulate and on feruloylated saccharides. The unprecedented substrate profile of Rs pCAE together with the lack of sequence similarity to known FAEs or pCAEs suggested that the Rs pCAE represents a new type of enzyme. Hydroxycinnamic acids were released from agro-industrial side-streams, such as destarched wheat bran (DSWB), sugar beet pectin (SBP) and coffee pulp (CP). Overnight incubation of coffee pulp with the Rs pCAE resulted in the efficient release of p-coumaric (100%), caffeic (100%) and ferulic acid (85%) indicating possible applications for the valorization of food processing wastes and for the enhanced degradation of lignified biomass.

Keywords

    Agro-industrial by-products, Basidiomycota, Chlorogenic acid, Feruloyl esterase, Feruloylated saccharides, Heterologous expression, Pichia pastoris

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A p-coumaroyl esterase from Rhizoctonia solani with a pronounced chlorogenic acid esterase activity. / Nieter, Annabel; Kelle, Sebastian; Linke, Diana et al.
In: New biotechnology, Vol. 37, 31.01.2017, p. 153-161.

Research output: Contribution to journalArticleResearchpeer review

Nieter A, Kelle S, Linke D, Berger RG. A p-coumaroyl esterase from Rhizoctonia solani with a pronounced chlorogenic acid esterase activity. New biotechnology. 2017 Jan 31;37:153-161. doi: 10.1016/j.nbt.2017.01.002
Nieter, Annabel ; Kelle, Sebastian ; Linke, Diana et al. / A p-coumaroyl esterase from Rhizoctonia solani with a pronounced chlorogenic acid esterase activity. In: New biotechnology. 2017 ; Vol. 37. pp. 153-161.
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AU - Nieter, Annabel

AU - Kelle, Sebastian

AU - Linke, Diana

AU - Berger, Ralf G.

PY - 2017/1/31

Y1 - 2017/1/31

N2 - Extracellular esterase activity was detected in submerged cultures of Rhizoctonia solani grown in the presence of sugar beet pectin or Tween 80. Putative type B feruloyl esterase (FAE) coding sequences found in the genome data of the basidiomycete were heterologously expressed in Pichia pastoris. Recombinant enzyme production on the 5-L bioreactor scale (Rs pCAE: 3245 U L−1) exceeded the productivity of the wild type strain by a factor of 800. Based on substrate specificity profiling, the purified recombinant Rs pCAE was classified as a p-coumaroyl esterase (pCAE) with a pronounced chlorogenic acid esterase side activity. The Rs pCAE was also active on methyl cinnamate, caffeate and ferulate and on feruloylated saccharides. The unprecedented substrate profile of Rs pCAE together with the lack of sequence similarity to known FAEs or pCAEs suggested that the Rs pCAE represents a new type of enzyme. Hydroxycinnamic acids were released from agro-industrial side-streams, such as destarched wheat bran (DSWB), sugar beet pectin (SBP) and coffee pulp (CP). Overnight incubation of coffee pulp with the Rs pCAE resulted in the efficient release of p-coumaric (100%), caffeic (100%) and ferulic acid (85%) indicating possible applications for the valorization of food processing wastes and for the enhanced degradation of lignified biomass.

AB - Extracellular esterase activity was detected in submerged cultures of Rhizoctonia solani grown in the presence of sugar beet pectin or Tween 80. Putative type B feruloyl esterase (FAE) coding sequences found in the genome data of the basidiomycete were heterologously expressed in Pichia pastoris. Recombinant enzyme production on the 5-L bioreactor scale (Rs pCAE: 3245 U L−1) exceeded the productivity of the wild type strain by a factor of 800. Based on substrate specificity profiling, the purified recombinant Rs pCAE was classified as a p-coumaroyl esterase (pCAE) with a pronounced chlorogenic acid esterase side activity. The Rs pCAE was also active on methyl cinnamate, caffeate and ferulate and on feruloylated saccharides. The unprecedented substrate profile of Rs pCAE together with the lack of sequence similarity to known FAEs or pCAEs suggested that the Rs pCAE represents a new type of enzyme. Hydroxycinnamic acids were released from agro-industrial side-streams, such as destarched wheat bran (DSWB), sugar beet pectin (SBP) and coffee pulp (CP). Overnight incubation of coffee pulp with the Rs pCAE resulted in the efficient release of p-coumaric (100%), caffeic (100%) and ferulic acid (85%) indicating possible applications for the valorization of food processing wastes and for the enhanced degradation of lignified biomass.

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