Acidic-alkaline ferulic acid esterase from Chaetomium thermophilum var. dissitum: Molecular cloning and characterization of recombinant enzyme expressed in Pichia pastoris

Gleb Dotsenko, Xiaoxue Tong, Bo Pilgaard, Peter Kamp Busk, Lene Lange

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

A novel ferulic acid esterase encoding gene CtFae, was successfully cloned from a highly esterase active strain of the thermophile ascomycetous fungus Chaetomium thermophilum var. dissitum; the gene was heterologously expressed in Pichia pastoris KM71H. The recombinant enzyme (CtFae) was purified to homogeneity and subsequently characterized. CtFae was active towards synthetic esters of ferulic, p-coumaric, and caffeic acids, as well as towards wide range of p-nitrophenyl substrates. Its temperature and pH optima were 55 °C and pH 6.0, respectively. Enzyme rare features were broad pH optimum, high stability at extended acidic-alkaline pH region, and noticeable thermostability. CtFae released ferulic acid from wheat insoluble arabinoxylan, as well as ferulic and p-coumaric acids from wheat straw and ryegrass, indicating potentials for industrial applications like biomass conversion in biorefineries.
Original languageEnglish
JournalBiocatalysis and Agricultural Biotechnology
Volume5
Pages (from-to)48-55
ISSN1878-8181
DOIs
Publication statusPublished - 2016

Keywords

  • Chaetomium thermophilum
  • Ferulic acid esterase
  • Hydroxycinnamic acids
  • Wheat straw
  • Arabinoxylan

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