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RISS 인기검색어
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- 저자 : Keshab Chandra Mondal (검색결과 2 건)
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Folk to functional: An explorative overview of rice-based fermented foods and beverages in India
Mousumi Ray,Kuntal Ghosh,Somnath Singh,Keshab Chandra Mondal 한국식품연구원 2016 Journal of Ethnic Foods Vol.3 No.1
Fermented foods share an integral part of age-old wisdom from ancient Indian civilization. Over the generations, this pioneering practice of food fermentation has expanded and improved to preserve and fortify the available food resources, particularly to meet the hidden hunger. India, being the second largest producer of rice, has a great history of traditional rice-based fermented foods with different tastes and textures linked with cultural diversity and mostly prepared by rural women following village art techniques. Some of them have been scientifically investigated and it has been revealed that microflora in natural or starter culture plays imperative roles to bio-embolden the rice with varieties of health promoting macronutrients and micronutrients, phytochemicals, and other functional components during fermentation. In this review, some explorative information on traditional rice-based foods and beverages has been assembled to illustrate the global interest in Indian food heritage and their functional aspects. The review also deals with the preparation of raw materials, traditional processing, composition, and ethno-medicinal importance of each food to encourage entrepreneurs to develop large-scale production to meet the growing market demand of functional foods.
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Amrita Banerjee,Pradeep Kumar Das Mohapatra,Shilpee Pal,Keshab Chandra Mondal,Bikash Ranjan Pati,Arnab Sen,Tanmay Paul 셀메드 세포교정의약학회 2014 TANG Vol.4 No.1
Anthrax is the deadly disease for human being caused by Bacillus anthracis. Instantaneous research work on the mode of infection of the organism revealed that different proteases are involved in different steps of pathogenesis. Present study reports the in silico characterization and the detection of pathogenic proteases involved in anthrax infection through protein-protein interaction. A total of 13 acid, 9 neutral, and 1 alkaline protease of Bacillus anthracis were selected for analysing the physicochemical parameter, the protein superfamily and family search, multiple sequence alignment, phylogenetic tree construction, protein-protein interactions and motif finding. Among the 13 acid proteases, 10 were found as extracellular enzymes that interact with immune inhibitor A (InhA) and help the organism to cross the blood brain barrier during the process of infection. Multiple sequence alignment of above acid proteases revealed the position 368, 489, and 498-contained 100% conserved amino acids which could be used to deactivate the protease. Among the groups analyzed, only acid protease were found to interact with InhA, which indicated that metalloproteases of acid protease group have the capability to develop pathogenesis during B. anthracis infection. Deactivation of conserved amino acid position of germination protease can stop the sporulation and germination of B anthracis cell. The detailed interaction study of neutral and alkaline proteases could also be helpful to design the interaction network for the better understanding of anthrax disease.
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