A new generation of flowerlike horseradish peroxides as a nanobiocatalyst for superior enzymatic activity

ÖÇSOY I., DOGRU E., USTA S.

ENZYME AND MICROBIAL TECHNOLOGY, ss.25-29, 2015 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Basım Tarihi: 2015
  • Doi Numarası: 10.1016/j.enzmictec.2015.04.010
  • Dergi Adı: ENZYME AND MICROBIAL TECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.25-29
  • Anahtar Kelimeler: HRP, Iron ion, Catalytic activity, Stability, Hybrid nanoflower, GRAPHENE OXIDE, IMMOBILIZATION, NANOPARTICLES, ENZYMES, PROTEIN, NANOFLOWERS, PLATFORM
  • Erciyes Üniversitesi Adresli: Evet

Özet

Although various supports including nanomaterials have been widely utilized as platforms for enzymes immobilization in order to enhance their catalytic activities, most of immobilized enzymes exhibited reduced activities compared to free enzymes. In this study, for the first time, we used iron ions (Fe2+) and horseradish peroxidase (HRP) enzyme together to synthesize flowerlike hybrid nanostructures with greatly enhanced activity and stability and reported an explanation of the enhancements in both catalytic activity and stability. We demonstrated that Fe2*-HRP hybrid nanoflower (HNF) showed catalytic activity of similar to 512% and similar to 710%, respectively when stored at +4 degrees C and room temperature (RT = 20 degrees C) compared to free HRP. In addition, the HNF stored at +4 degrees C lost only 2.9% of its original activity within 30 days while the HNF stored at RT lost approximately 10% of its original activity. However, under the same conditions, free HRP enzymes stored at +4 degrees C and RT lost 68% and 91% of their activities, respectively. We claim that the drastic increases in activities of HNF are associated with to high local HRP concentration in nanoscale dimension, appropriate HRP conformation, less mass transfer limitations, and role of Fe2+ ion as an activator for HRP. Further biosensors studies based on enhanced activity and stability of HNF are currently underway. (C) 2015 Elsevier Inc. All rights reserved.

Although various supports including nanomaterials have been widely utilized as platforms for enzymes immobilization in order to enhance their catalytic activities, most of immobilized enzymes exhibited reduced activities compared to free enzymes. In this study, for the first time, we used iron ions (Fe2+) and horseradish peroxidase (HRP) enzyme together to synthesize flowerlike hybrid nanostructures with greatly enhanced activity and stability and reported an explanation of the enhancements in both catalytic activity and stability. We demonstrated that Fe2+-HRP hybrid nanoflower (HNF) showed catalytic activity of ∼512% and ∼710%, respectively when stored at +4 °C and room temperature (RT = 20 °C) compared to free HRP. In addition, the HNF stored at +4 °C lost only 2.9% of its original activity within 30 days while the HNF stored at RT lost approximately 10% of its original activity. However, under the same conditions, free HRP enzymes stored at +4 °C and RT lost 68% and 91% of their activities, respectively. We claim that the drastic increases in activities of HNF are associated with to high local HRP concentration in nanoscale dimension, appropriate HRP conformation, less mass transfer limitations, and role of Fe2+ ion as an activator for HRP. Further biosensors studies based on enhanced activity and stability of HNF are currently underway.