Separation of catalase from Amsonia orientalis with single step by aqueous two-phase partitioning system (ATPS)

Duman Y., ACEMİ A., Yuzugullu Y., ÖZEN F.

SEPARATION SCIENCE AND TECHNOLOGY, cilt.52, sa.4, ss.691-699, 2017 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 52 Sayı: 4
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1080/01496395.2016.1253588
  • Dergi Adı: SEPARATION SCIENCE AND TECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.691-699
  • Anahtar Kelimeler: ATPS, aqueous two-phase partitioning, catalase, extraction, purification, recovery, PURIFICATION, EXTRACTION, PROTEINS, RECOVERY, BEHAVIOR
  • Kocaeli Üniversitesi Adresli: Evet

Özet

Catalase from Amsonia orientalis was purified by ATPS, and its efficiency was compared against hydrophobic interaction chromatography. Activity recovery and purification fold of purified catalase by ATPS were examined under varying experimental conditions. The effects of various factors such as type of phase-forming salts, (PEG) mass, with their different concentrations, pH and temperature effects on partitioning were investigated. The highest activity recovery (156%) and purification fold (8.67) of catalase were obtained in the ATPS system containing 10% (g/g) PEG4000, 15% (g/g) Na2SO4 at pH 6.0 and room temperature. In hydrophobic interaction chromatography, the enzyme has been purified 12.54-fold with 57.5% recovery. The molecular weight of catalase was determined as 75 kDa by SDS-PAGE.