A halotolerant type A feruloyl esterase from Pleurotus eryngii

verfasst von

Annabel Nieter, Paul Haase-Aschoff, Diana Linke, Manfred Nimtz, Ralf G. Berger

Abstract

An extracellular feruloyl esterase (PeFaeA) from the culture supernatant of Pleurotus eryngii was purified to homogeneity using cation exchange, hydrophobic interaction, and size exclusion chromatography. The length of the complete coding sequence of PeFaeA was determined to 1668 bp corresponding to a protein of 555 amino acids. The catalytic triad of Ser-Glu-His demonstrated the uniqueness of the enzyme compared to previously published FAEs. The purified PeFaeA was a monomer with an estimated molecular mass of 67kDa. Maximum feruloyl esterase (FAE) activity was observed at pH 5.0 and 50°C, respectively. Metal ions (5mM), except Hg²⁺, had no significant influence on the enzyme activity. Substrate specificity profiling characterized the enzyme as a type A FAE preferring bulky natural substrates, such as feruloylated saccharides, rather than small synthetic ones. K_m and k_cat of the purified enzyme for methyl ferulate were 0.15mM and 0.85s^-1. In the presence of 3M NaCl activity of the enzyme increased by 28%. PeFaeA alone released only little ferulic acid from destarched wheat bran (DSWB), whereas after addition of Trichoderma viride xylanase the concentration increased more than 20 fold.

Organisationseinheit(en)

Institut für Lebensmittelchemie

Externe Organisation(en)

Helmholtz-Zentrum für Infektionsforschung GmbH (HZI)

Typ

Artikel

Journal

Fungal biology

Band

118

Seiten

348-357

Anzahl der Seiten

10

ISSN

1878-6146

Publikationsdatum

06.02.2014

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Ökologie, Evolution, Verhaltenswissenschaften und Systematik, Genetik, Infektionskrankheiten

Ziele für nachhaltige Entwicklung

SDG 3 – Gute Gesundheit und Wohlergehen

Elektronische Version(en)

https://doi.org/10.1016/j.funbio.2014.01.010 (Zugang: Geschlossen)