Characterization of β-xylosidase enzyme from a Pichia stipitis mutant


Basaran P., Ozcan M.

Bioresource Technology, cilt.99, sa.1, ss.38-43, 2008 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 99 Sayı: 1
  • Basım Tarihi: 2008
  • Doi Numarası: 10.1016/j.biortech.2006.11.056
  • Dergi Adı: Bioresource Technology
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.38-43
  • Anahtar Kelimeler: β-Xylosidase, Mutant, Pichia stipitis
  • İstanbul Teknik Üniversitesi Adresli: Hayır

Özet

β-Xylosidase production was maximal for the mutant Pichia stipitis NP54376 grown on xylan as the sole carbon source. β-Xylosidase was purified from culture supernatant by (NH4)2SO4 precipitation and a hydrophobic interaction chromatography on phenyl sepharose. Optima of pH and temperature were 5.0 and 50 °C, respectively. The enzyme was inhibited by 2-mercaptoethanol (100%) and Fe3+ (80%), and moderately affected by Cu2+, Ag+, NH4+ and Mg2+ and SDS. The purified xylosidase hydrolyzed xylobiose and xylo-oligosaccharides and it did not exhibit activity against cellulose, starch, maltose and cellobiose. 2.5 g l-1 glucose repressed β-xylosidase activity in the NP54376 strain. The Km and Vmax values on p-nitrophenyl-β-xylopyranoside were 1.6 mM and 186 μmol p-nitrophenyl min-1 mg-1 protein, respectively. Analysis of the hydrolysis products by HPLC indicated that the major hydrolysis product is xylobiose in all the carbon sources tested. © 2006 Elsevier Ltd. All rights reserved.