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Purification and characterization of Mn-peroxidase from <i style="">Musa paradisiaca</i> (banana) stem juice

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Title Purification and characterization of Mn-peroxidase from Musa paradisiaca (banana) stem juice
 
Creator Yadav, Pratibha
Singh, V K
Yadav, Meera
Singh, Sunil Kumar
Yadava, Sudha
Yadav, K D S
 
Subject Mn-Peroxidase
Metalloenzyme
Musa Paradisiaca
Banana
Plant Peroxidase
Heme-Enzyme
Bromination Reaction
 
Description 42-48
Mn-peroxidase
(MnP), a biotechnologically important enzyme was purified for the first time from
a plant source Musa paradisiaca (banana) stem, which is an agro-waste
easily available after harvest of banana fruits. MnP was earlier purified only
from the fungal sources. The enzyme was purified from stem juice by
ultrafiltration and anion-exchange column chromatography on diethylamino
ethylcellulose with 8-fold purification and purification yield of 65%. The
enzyme gave a single protein band in SDS-PAGE corresponding to molecular mass
43 kDa. The Native-PAGE of the enzyme also gave a single protein band,
confirming the purity of the enzyme. The UV/VIS spectrum of the purified enzyme
differed from the other heme peroxidases, as the Soret band was shifted towards
lower wavelength and the enzyme had an intense absorption band around 250 nm. The
Km values using MnSO4
and H2O2 as the substrates of the purified enzyme were
21.0 and 9.5 μM, respectively. The calculated kcat value of the purified enzyme using Mn(II) as the
substrate in 50 mM lactate buffer (pH
4.5) at 25°C was 6.7s-1, giving a kcat/Km value
of 0.32 μM-1s-1. The kcat
value for the MnP-catalyzed reaction was found to be dependent of the Mn(III)
chelator molecules malonate, lactate and oxalate, indicating that the enzyme
oxidized chelated Mn(II) to Mn(III). The pH
and temperature optima of the enzyme were 4.5 and 25°C, respectively. The enzyme in combination with
H2O2 liberated bromine and iodine in presence of KBr and
KI respectively. All these enzymatic characteristics were similar to those of
fungal MnP. The enzyme has the potential as a green brominating and iodinating
agent in combination with KBr/KI and H2O2.
 
Date 2012-02-14T12:28:00Z
2012-02-14T12:28:00Z
2012-02
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/13590
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.49(1) [February 2012]