Open AccessHeterologous production of a laccase from the basidiomycete Pycnoporus cinnabarinus in the dimorphic yeast Yarrowia lipolytica
Author(s) -
Madzak Catherine,
Otterbein Ludovic,
Chamkha Mohamed,
Moukha Serge,
Asther Marcel,
Gaillardin Claude,
Beckerich JeanMarie
Publication year - 2005
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1016/j.femsyr.2004.10.009
Subject(s) - yarrowia , biology , yeast , transformation (genetics) , laccase , bioreactor , heterologous , biochemistry , mycelium , recombinant dna , pichia pastoris , pichia , microbiology and biotechnology , gene , enzyme , botany
Pycnoporus cinnabarinus lac1 gene was expressed in Yarrowia lipolytica . Different secretion signals and culture media were tested. Production was correlated to both culture growth rate and cell morphology (highest at low growth rate, without mycelium). Recombinant laccase was characterized (immunodetection, N‐terminal sequencing) and purified. Production was estimated to 20 mg l −1 in a bioreactor. Thus, complex metalloenzymes can be produced in Yarrowia , assuming some control of host physiology. Lac1p production was compared in Yarrowia , Pichia and Aspergillus : recombinant proteins were active, but host systems differed in transformation efficiency, production, and glycosylation. If not the best producer, Yarrowia offers very high transformation efficiencies, allowing the genetic engineering of laccases for industrial applications.