Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH

Binay B., ALAGÖZ D., YILDIRIM D., Celik A., TÜKEL S. S.

BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY, cilt.12, ss.271-277, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 12
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3762/bjoc.12.29
  • Dergi Adı: BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.271-277
  • Anahtar Kelimeler: biocatalysis, Candida methylica, formate dehydrogenase, Immobead 150, regeneration of NADH, stabilization, OLD YELLOW ENZYME, COVALENT IMMOBILIZATION, CANDIDA-BOIDINII, EPOXY SUPPORTS, PURIFICATION, REDUCTION, REACTOR, DESIGN, SYSTEM, SCALE
  • Çukurova Üniversitesi Adresli: Evet

Özet

This study aimed to prepare robust immobilized formate dehydrogenase (FDH) preparations which can be used as effective biocatalysts along with functional oxidoreductases, in which in situ regeneration of NADH is required. For this purpose, Candida methylica FDH was covalently immobilized onto Immobead 150 support (FDHI150), Immobead 150 support modified with ethylenediamine and then activated with glutaraldehyde (FDHIGLU), and Immobead 150 support functionalized with aldehyde groups (FDHIALD). The highest immobilization yield and activity yield were obtained as 90% and 132%, respectively when Immobead 150 functionalized with aldehyde groups was used as support. The half-life times (t(1/2)) of free FDH, FDHI150, FDHIGLU and FDHIALD were calculated as 10.6, 28.9, 22.4 and 38.5 h, respectively at 35 degrees C. FDHI150, FDHIGLU and FDHIALD retained 69, 38 and 51% of their initial activities, respectively after 10 reuses. The results show that the FDHI150, FDHIGLU and FDHIALD offer feasible potentials for in situ regeneration of NADH.