Isozyme variation areca catechu L. and allied species
By: Arul Swaminathan A.
Contributor(s): George T E (Guide).
Material type:
BookPublisher: Vellanikkara Department of Plantation Crops and Spices, College of Horticulture 2002DDC classification: 633.8 Online resources: Click here to access online Dissertation note: MSc Abstract: 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.
| Item type | Current location | Call number | Status | Date due | Barcode |
|---|---|---|---|---|---|
Theses
|
KAU Central Library, Thrissur Theses | 633.8 ARU/IS (Browse shelf) | Available | 171917 |
MSc
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.
There are no comments for this item.