A halotolerant type A feruloyl esterase from Pleurotus eryngii

authored by: 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.
Organisation(s): Institute of Food Chemistry
External Organisation(s): Helmholtz Centre for Infection Research (HZI)
Type: Article
Journal: Fungal biology
Volume: 118
Pages: 348-357
No. of pages: 10
ISSN: 1878-6146
Publication date: 06.02.2014
Publication status: Published
Peer reviewed: Yes
ASJC Scopus subject areas: Ecology, Evolution, Behavior and Systematics, Genetics, Infectious Diseases
Sustainable Development Goals: SDG 3 - Good Health and Well-being
Electronic version(s): https://doi.org/10.1016/j.funbio.2014.01.010 (Access: Closed)