Spongy membranes for peroxidase purification from Brassica oleracea roots

Pesint G. B., Zenger O., PERÇİN DEMİRÇELİK I., DENİZLİ A.

PROCESS BIOCHEMISTRY, cilt.103, ss.98-106, 2021 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 103
  • Basım Tarihi: 2021
  • Doi Numarası: 10.1016/j.procbio.2021.02.005
  • Dergi Adı: PROCESS BIOCHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aerospace Database, Aqualine, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Communication Abstracts, Compendex, Food Science & Technology Abstracts, INSPEC, Metadex, Pollution Abstracts, Veterinary Science Database, Civil Engineering Abstracts
  • Sayfa Sayıları: ss.98-106
  • Anahtar Kelimeler: Spongy membrane, 2-4-Vinylphenylboronic acid, Peroxidase, Enzyme purification, Cryogel
  • Hacettepe Üniversitesi Adresli: Evet

Özet

In this work, it was aimed to purify peroxidase from Brassica oleracea roots using newly synthesized cryogel membranes. 2-4-vinylphenylboronic acid (VPBA) containing 2-hydroxyethyl methacrylate (HEMA) [PHE-MABA] cryogel membranes were prepared successfully and swelling tests, scanning electron microscopy (SEM), Fourier-transform infrared (FTIR) spectroscopy, contact angle measurements, and Brauner-Emmet-Teller (BET) surface area analysis were done for characterization. Effect of experimental conditions on peroxidase binding capacity of PHEMABA cryogel membranes was determined by examining parameters such as pH, temperature and time with binding studies. Maximum peroxidase binding capacity of PHEMABA cryogel membranes was determined as 22.01 mg/g for 2 mg/mL equilibrium peroxidase concentration at pH 8.0. Finally, peroxidase was purified from Brassica oleracea roots with 85.38% yield and 18.38 purification fold. According to obtained re-sults, spongy PHEMABA cryogel membranes show high peroxidase binding capacity and could be suggested as a boronate affinity model system for enzyme purification.