Record Details

Purification and characterization of cinnamyl alcohol-NADPH-dehydrogenase from the leaf tissues of a basin mangrove Lumnitzera racemosa Willd.

NOPR - NISCAIR Online Periodicals Repository

View Archive Info
 
 
Field Value
 
Title Purification and characterization of cinnamyl alcohol-NADPH-dehydrogenase from the leaf tissues of a basin mangrove Lumnitzera racemosa Willd.
 
Creator Murugan, K
Arunkumar, N S
Mohankumar, C
 
Subject Lumnitzera racemosa
Cinnamyl alcohol-NADPH-dehydrogenase
Basin mangrove.
 
Description 96-101
• Cinnamyl alcohol-NADPH-dehydrogenase (CAD), the marker enzyme of lignin biosynthesis was purified from the leaf tissues of a basin mangrove Lumnitzera racemosa by ammonium sulphate precipitation, followed by anion-exchange, gel filtration and affinity chromatography. The molecular mass of the CAD enzyme was determined as 89 kDa, by size elution chromatography. SDS-PAGE of CAD revealed two closely associated bands of 45 kDa and 42 kDa as heterogenous subunits. The optimum pH of CAD was found to be 4.0. Km for the substrates cinnamaldehyde, coniferaldehyde and sinapaldehyde was determined. Cinnamaldehyde showed higher Km value than sinapaldehyde and coniferaldehyde. The correlation of activity of CAD with the amount of lignin was found less significant in L. racemosa, compared to plant species of other habitats viz., mesophytes, xerophytes and hydrophytes, suggesting that CAD possibly exhibits physiological suppression due to the saline habitat of the plant.
 
Date 2009-03-31T10:45:01Z
2009-03-31T10:45:01Z
2004-04
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3640
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol. 41(2 & 3) [April-June 2004]