TY  - BOOK
AU  - Arul Swaminathan A 
AU  - George T E (Guide)
TI  - Isozyme variation areca catechu L. and allied species
U1  - 633.8 
PY  - 2002///
CY  - Vellanikkara
PB  - Department of Plantation Crops and Spices, College of Horticulture
N2  - Investigations on "Isozyme variation 10 Areca catechu L. and allied 
species" were undertaken in the Department of Plantation Crops and Spices and the 
Biochemistry laboratory of the College of Horticulture, Kerala Agricultural 
University, Vellanikkara during the period from 2000 to 2002 with the major 
objectives of working out the species relationship in the genus Areca and 
biochemically characterizing the varieties/cultivars/types of arecanut by isozyme 
, 
	analysis. 	.:' 
Twenty four arecanut accessions comprising of four species, five released 
varieties, 12 traditional cultivars and three exotic cultivars collected from various 
states were included in the investigation. The isozymes studied were peroxidase, 
esterase and polyphenol oxidase. 
The species VIZ., Areca catechu, A. triandra, A. lutescens and A. 
normanbyii were displayed variations with respect to the isozyme banding 
patterns, while no variation was observed among the five released varieties. 
Traditional cultivars numbering 12 had shown very little variation except in the 
case of TC3 and TC10. The exotic cultivars, which included two YLD tolerant 
accessions, had shown a striking variation when compared to other accessions of A. 
catechu. Based on the banding pattern of all the isozymes, the accessions were 
classified into eight groups. The dendrogram plotted using cluster analysis also 
vindicated this classification. 
The protein content of the accessions ranged from 3.4 to 8.8 mg/ml extract. 
The protein content was very high in the YLD tolerant accessions when compared 
to the susceptible genotypes. The activity of the enzyme peroxidase recorded a 
wide range of 120 - 1455 units/ml while the range of polyphenol oxidase was 22 - 
208 units /ml. The activity values of peroxidase and polyphenol oxidase were very 
low in all the YLD tolerant lines in comparison with other accessions. High 
protein content alongwith low enzyme activity levels recorded invariably by all the 
tolerant accessions point towards a possible influence of these biochemical 
parameters on YLD tolerant reaction. 


UR  - http://krishikosh.egranth.ac.in/handle/1/5810036891
ER  -