Partial Purification and Characterization of Polyphenol Oxidase Enzyme from Common-Morning Glory (Ipomoea purpurea)

Yüzügüllü Karakuş Y., Kale E., Acemi A., Mansurov B.

KSU TARIM VE DOGA DERGISI-KSU JOURNAL OF AGRICULTURE AND NATURE, cilt.25, sa.1, ss.22-32, 2022 (ESCI) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 25 Sayı: 1
  • Basım Tarihi: 2022
  • Doi Numarası: 10.18016/ksutarimdoga.vi.1008243
  • Dergi Adı: KSU TARIM VE DOGA DERGISI-KSU JOURNAL OF AGRICULTURE AND NATURE
  • Derginin Tarandığı İndeksler: Emerging Sources Citation Index (ESCI), TR DİZİN (ULAKBİM)
  • Sayfa Sayıları: ss.22-32
  • Anahtar Kelimeler: Polyphenol oxidase, Three-phase partitioning, Enzyme purification, Characterization, Ipomoea purpurea, BIOCHEMICAL-CHARACTERIZATION, L., PEROXIDASE, STABILITY, PROTEIN
  • Kocaeli Üniversitesi Adresli: Evet

Özet

This study aimed to purify and biochemically characterize polyphenol oxidase (PPO) enzyme from the plant Ipomoea purpurea (I. purpurea) for the first time. For this purpose, the crude extract sample obtained from the extraction of in vitro cultured plant leaves under optimum conditions (25 mgmL(-1) Polyvinylpolypyrrolidone, pH 7.0) was subjected to three-phase partitioning, and the PPO enzyme was 10.5-fold purified with a 57% activity recovery. The optimum pH and temperature values were determined as 7.0 and 30 degrees C, respectively. Laccase, peroxidase, and catechol oxidase activities were observed after activity staining of partially purified enzyme. From stability tests, it was noted that more than 75% and 65% of its original activity were maintained at temperatures 20 degrees C-40 degrees C and pH 7.0-9.0, respectively.