Journalartikel

Jahr der Veröffentlichung: 2005

Seiten: 435-440

Zeitschrift: Biological Chemistry

Bandnummer: 386

Heftnummer: 5

ISSN: 1431-6730

DOI Link: https://doi.org/10.1515/BC.2005.052

Verlag: De Gruyter Brill

Abstract: 
An extracellular enzyme capable of efficient hydrolysis of xanthophyll esters was purified from culture supernatants of the basidiomycete Pleurotus sapidus. Under native conditions, the enzyme exhibited a molecular mass of 430 kDa, and SDS-PAGE data suggested a composition of eight identical subunits. Biochemical characterisation of the purified protein showed an isoelectric point of 4.5, and ideal hydrolysis conditions were observed at pH 5.8 and 40 degrees C. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. An 1861-bp cDNA containing an open reading frame of 1641 bp was cloned from a cDNA library that showed ca. 40% homology to Candida rugosa lipases. The P sapidus carboxylesterase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus that has been characterised at the molecular level.

Harvard-Zitierstil: Zorn, H., Bouws, H., Takenberg, M., Nimtz, M., Getzlaff, R., Breithaupt, D., et al. (2005) An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters, Biological Chemistry, 386(5), pp. 435-440. https://doi.org/10.1515/BC.2005.052

APA-Zitierstil: Zorn, H., Bouws, H., Takenberg, M., Nimtz, M., Getzlaff, R., Breithaupt, D., & Berger, R. (2005). An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters. Biological Chemistry. 386(5), 435-440. https://doi.org/10.1515/BC.2005.052