TY  - JOUR
TI  - Partial Purification and Characterization of Polyphenol Oxidase Enzyme from Common- Morning Glory (Ipomoea purpurea)
AB  - 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°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℃-40℃ and pH 7.0-9.0, respectively.
AU  - Kale Bakir, Elif
AU  - Acemi, Arda
AU  - Yuzugullu Karakus, Yonca
AU  - MANSUROV, Bektore
DO  - 10.18016/ksutarimdoga.vi.1008243
PY  - 2022
JO  - Kahramanmaraş Sütçü İmam Üniversitesi Tarım ve Doğa Dergisi
VL  - 25
IS  - Ek Sayı1
SN  - 2619-9149
SP  - 22
EP  - 32
DB  - TRDizin
UR  - http://search/yayin/detay/1171155
ER  -