Purification of chloroperoxidase from Musa paradisiaca stem juice

Abstract

Chloroperoxidase from Musa paradisiaca stem juice has been purified to homogeneity using a concentration obtained by ultrafiltration and anion exchange chromatography on diethylaminoethyl (DEAE) cellulose. The purified enzyme gave a single protein band in SDS-PAGE analysis corresponding to molecular mass of 43 kDa. The native PAGE analysis result has also given a single protein band, confirming the purity of the enzyme. The purified enzyme was chlorinated and brominated with monochlorodimedone, the substrate used for measuring the halogenating activity of chloroperoxidases. The K m and k cat values using monochlorodimedone as the substrate were 20 μM and 1.64 s −1 , respectively, giving a k cat /K m value of 8.2 × 10 4 M −1 s −1 . The pH and temperature optima of the chlorinating activity were 3.0 and 25 • C, respectively. The K m values for the peroxidase activity using pyragallol and H 2 O 2 as the variable substrates were 89 and 120 μM, respectively. The pH and temperature optima of the peroxidase activity using pyrogalllol as the substrate were the same as the pH and temperature optima of the halogenating activity. The peroxidase activity of the enzyme is competitively inhibited by sodium azide, indicating that it is a hemeperoxidase different from nonheme peroxidases.

Extraction, purification and processing stability of peroxidase from plums (Prunus domestica)

“…In the range 40-60°C, the process of thermal inactivation begins although the enzymatic activity does not decrease significantly. The results obtained for POD from plums are in accordance with the study of Yadav et al [26] who investigated the POD from banana (Musa paradisiaca) in the 15-35°C temperature range, and reported the optimum temperature of 25°C. In contrast, Rani and Abraham [15] determined the optimum temperature of 55°C for the activity of POD from Eupatorium odoratum, whereas Pandey and Dwivedi [4] studied POD from papaya and assessed an optimum temperature of 40°C.…”

Partial Purification and Characterization of Peroxidase from Pearl Millet (Pennisetum Glaucum [L.] R. Br.) Grains

“…() and Yadav et al . () also reported that peroxidase had an optimum temperature of 25C. The enzyme from lettuce stem showed an optimum temperature of 45C (Hu et al .…”

Multi-way Degradation and Process Optimization of Phenol from Simulated Wastewater System

“…These enzymes include Peroxidase, Chloroperoxidase, Lignin peroxidase, Mnperoxidase [9] and catalase [10] that isolated from specific plants viz. soybean [11], horseradish, radish [12], and their materials such as seeds [13], leaves [14], stem [15], roots [16]. Tyrosinase and Laccase [9] are obtained from different fungal species.…”