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Kumaria, Suman
- Artificial Seed for Short-Term Storage:Using Nodal Buds in Aquilaria malaccensis Lam
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Authors
Affiliations
1 Plant Biotechnology Laboratory, Department of Botany, North-Eastern Hill University, Shillong 793 022, IN
1 Plant Biotechnology Laboratory, Department of Botany, North-Eastern Hill University, Shillong 793 022, IN
Source
Current Science, Vol 115, No 11 (2018), Pagination: 2103-2109Abstract
Artificial seed technology is known to be the best alternative for short-term storage of plant germplasm in recalcitrant species. Aquilaria malaccensis, being a recalcitrant seeded tree, possesses seasonal and highly desiccation-sensitive seeds which lose viability with slight decrease in their moisture content, hence storage becomes a difficult task. The present study deals with short-term storage of A. malaccensis nodal buds through artificial seed technology. Nodal buds encapsulated with 2.5% sodium alginate and 100 mM calcium chloride, and polymerized for 40 min were found suitable for artificial seed preparation. Maximum regeneration rate of 83.3% and 75.0% was observed from encapsulated nodal buds stored at 4°C and 23 ± 2°C respectively, for 10 days. Storage was possible for a period of 60 days at 4°C and 50 days at 23 ± 2°C with average regeneration rate of 8.3% and 16.7% respectively.Keywords
Artificial Seeds, Encapsulation, Recalcitrant, Storage, Temperature.Full Text
References
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- Molecular Docking Study of CHS Gene from a Medicinally Important Orchid, Coelogyne ovalis Lindl.
Abstract Views :115 |
PDF Views:29
Authors
Nutan Singh
1,
Suman Kumaria
1
Affiliations
1 Department of Botany, Plant Biotechnology Laboratory, North-Eastern Hill University, Shillong 793 022, IN
1 Department of Botany, Plant Biotechnology Laboratory, North-Eastern Hill University, Shillong 793 022, IN
Source
Current Science, Vol 121, No 10 (2021), Pagination: 1323-1327Abstract
Chalcone synthase (CHS) is an important enzyme belonging to the polyketide synthase (type III) family. It is well known for substrate specificity and catalyses diverse groups of polyketides of pharmaceutical value. In the present study, the structure of the CHS protein has been predicted from the medicinal orchid, Coelogyne ovalis Lindl. This is an evergreen orchid, well known for its medicinal uses. The homology-based model was constructed from CHS of C. ovalis (CoCHS) and 16 different ligands were used based on the specificity for molecular docking studies. The four best ligands on the basis of greater negative binding energy were found to be 3-carbomoyl-picoliniyl CoA, followed by carbomoyl-2-napthoyl CoA, p-coumaroyl CoA and malonyl CoA. The present structural study reveals that CoCHS has signature and catalytic amino acid residues, namely Cys165, Asn337, His 306, Phe216 and Phe 266. These residues are known to have a broad-range substrate profile and are responsible for the binding of protein ligands. The present study elucidates the chemical basis of CHS from C. ovalis by understanding the structural and functional relationship. This provides an insight for manipulating the enzymes, CHS-like for the synthesis of new bioactive compounds, which may further enhance the diversity of the polyketide biosynthetic familyKeywords
Coelogyne ovalis, Chalcone Synthase, Ligands, Molecular Docking, Polyketides.Full Text
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