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IN SILICO CHARACTERIZATION OF RIPENING PROTEINS IN MUSA ACCUMINATA
Authors: Mishra S.K., Dwivedi S.P., Dwivedi N., Singh R. K., Dubey K.B
Number of views: 339
Musa accuminata is the member of family Musaceae. The fruits of M. accuminata are harvested in unriped green in order to better withstand transportation and to slow down the natural ripening process because of several weeks travel from the production areas to the end markets. The ripening process is a multi-step reaction involves a number of complex enzymes. The present work is aimed to computational characterization of these ripening enzymes in order to understand the ripening mechanism. In this work identification of the enzymes/proteins involved in ripening process are characterized by their conserved domains (conserved, 3-dimension region). The domains are identified by using the computational tool, CDART (Conserved Domain Architecture Retrieval Tool). By using this applied approach a number of conserved domains were identified, out of these enzymes, the domain pattern of Aspartate aminotransferase (AAT_Like), Glycosyl hydrolase (Glyco_Hydr) and oxoglutarate (20G_Fe) were reported the most conserved followed by Ethylene insensitive (EIN3), GT1, DPBB & Pollen in ripening enzyme complexes. The data, thus, obtained provide new insights in order to understand the role of the proteins playing in different stages of ripening process. These results provide a basis for further studies on the molecular mechanism of ripening process and food technological applications for delayed ripening in fruits, where ripening proteins plays an important role in.