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

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

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

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OriginalspracheEnglisch
Seiten (von - bis)153-161
Seitenumfang9
FachzeitschriftNew biotechnology
Jahrgang37
PublikationsstatusVeröffentlicht - 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.

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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, Jahrgang 37, 31.01.2017, S. 153-161.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-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 ; Jahrgang 37. S. 153-161.
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T1 - A p-coumaroyl esterase from Rhizoctonia solani with a pronounced chlorogenic acid esterase activity

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.

KW - Agro-industrial by-products

KW - Basidiomycota

KW - Chlorogenic acid

KW - Feruloyl esterase

KW - Feruloylated saccharides

KW - Heterologous expression

KW - Pichia pastoris

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DO - 10.1016/j.nbt.2017.01.002

M3 - Article

C2 - 28159727

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VL - 37

SP - 153

EP - 161

JO - New biotechnology

JF - New biotechnology

SN - 1871-6784

ER -