ArticlePhysiology and molecular biology of plants : an international journal of functional plant biology2023
Ethrel-induced release of fresh seed dormancy causes remodelling of amylase activity, proteomics, phytohormone and fatty acid profile of groundnut
Article in Physiology and molecular biology of plants : an international journal of functional plant biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 7 citations in OpenAlex.
- Enhancing flavor and oxidation stability of roasted peanut oil via germination pretreatment.Food chemistry: X · 2026Article
- Nutritional analysis of vegetable soybean [Frontiers in nutrition · 2025Article
- Methodological and Physiological Study during Seed Dormancy Release ofPlants (Basel, Switzerland) · 2024Article
- Physiological and molecular changes of onion (Allium cepa L.) seeds under different aging conditions.BMC plant biology · 2024Article
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Authors and funding
11 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
It is important to have a short period of fresh seed dormancy in some of the groundnut species to counter pre-harvest sprouting (PHS). One of the main causes of PHS is the activation of ethylene-mediated pathways. To determine the effect of ethylene, the study was conducted and alterations in amylase, proteins and fatty acids were observed at the 0, 6, 12, and 24 h stages after ethrel administration. The result showed an increase in amylase activity, and the fatty acids profile showed a unique alteration pattern at different germination stages. Two-dimensional gel electrophoresis (2DGE) revealed differential expression of proteins at each stage. The trypsin digestion following spectral development through UPLC-MS/MS enabled identification of number of differentially expressed proteins. A total of 49 proteins were identified from 2DGE excised spots. The majority were belonged to seed storage-related proteins like Arah1, Arah2, AAI- domain containing protein, conglutin, Arah3/4, arachin, glycinin. Expression of Supplementary Information: The online version contains supplementary material available at 10.1007/s12298-023-01332-6.
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