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Assam Agricultural University, Jorhat

Assam Agricultural University is the first institution of its kind in the whole of North-Eastern Region of India. The main goal of this institution is to produce globally competitive human resources in farm sectorand to carry out research in both conventional and frontier areas for production optimization as well as to disseminate the generated technologies as public good for benefitting the food growers/produces and traders involved in the sector while emphasizing on sustainability, equity and overall food security at household level. Genesis of AAU - The embryo of the agricultural research in the state of Assam was formed as early as 1897 with the establishment of the Upper Shillong Experimental Farm (now in Meghalaya) just after about a decade of creation of the agricultural department in 1882. However, the seeds of agricultural research in today’s Assam were sown in the dawn of the twentieth century with the establishment of two Rice Experimental Stations, one at Karimganj in Barak valley in 1913 and the other at Titabor in Brahmaputra valley in 1923. Subsequent to these research stations, a number of research stations were established to conduct research on important crops, more specifically, jute, pulses, oilseeds etc. The Assam Agricultural University was established on April 1, 1969 under The Assam Agricultural University Act, 1968’ with the mandate of imparting farm education, conduct research in agriculture and allied sciences and to effectively disseminate technologies so generated. Before establishment of the University, there were altogether 17 research schemes/projects in the state under the Department of Agriculture. By July 1973, all the research projects and 10 experimental farms were transferred by the Government of Assam to the AAU which already inherited the College of Agriculture and its farm at Barbheta, Jorhat and College of Veterinary Sciences at Khanapara, Guwahati. Subsequently, College of Community Science at Jorhat (1969), College of Fisheries at Raha (1988), Biswanath College of Agriculture at Biswanath Chariali (1988) and Lakhimpur College of Veterinary Science at Joyhing, North Lakhimpur (1988) were established. Presently, the University has three more colleges under its jurisdiction, viz., Sarat Chandra Singha College of Agriculture, Chapar, College of Horticulture, Nalbari & College of Sericulture, Titabar. Similarly, few more regional research stations at Shillongani, Diphu, Gossaigaon, Lakhimpur; and commodity research stations at Kahikuchi, Buralikson, Tinsukia, Kharua, Burnihat and Mandira were added to generate location and crop specific agricultural production packages.

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20192
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Author: Gupta, Rubi × End date: 2019 × Start date: 2017 × Type: Thesis × Thesis Type: Ph.D ×
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    ThesisItemOpen Access
    Molecular characterization and nutritional equivalence evaluation of transgenic chickpea expressing either a cry1Ac or cry2Aa gene
    (AAU, Jorhat, 2019-10) Gupta, Rubi; Sarmah, Bidyut Kumar
    Biosafety assessment of transgenic chickpeas having B.thuringiensis genes for resistance to pod borers is a regulatory requirement and mandatory to document before releasing in the field. Therefore, Bt chickpea lines harbouring either a cry1Ac or cry2Aa gene were characterized for the presence and expression of the transgene in their advanced generations, biosafety assessments and transcript profile were studied. The homozygous lines were selected for comparative nutritional equivalence assay. Biochemical estimations of major nutritional components such as proximates, vitamins, minerals, fatty acids and anti nutrients confirmed that the Bt chickpeas lines are nutritionally equivalent to their non-transgenic counterparts and the seed composition is similar or within the range reported, previously. Seed protein quality was investigated by separating the proteins in PAGE and eluted proteins after mass spectrometry (MS) showed expected fractions of 11S legumin, 7S vicilin, and 2S albumin of chickpea storage proteins in the transgenic lines. The protein digestibility was assayed using the multi-enzyme system and transient pepsin hydrolysis to mimic simulated gastric fluid followed by trypsin hydrolysis to mimic simulated intestinal fluid. Total seed proteins of both the transgenic and nontransgenic lines were digested at a similar rate and enzyme-resistant peptides were not observed in transgenic Bt chickpea lines. The unintended changes in the whole transcriptome profile of Bt chickpeas were surveyed using a homozygous transgenic line expressing a cry1Ac gene. The differentially expressed genes (DEGs) profiling confirmed a low (0.69%, log2fold change≥2) frequency of differentially expressed in the transgenic chickpea line. Only a small (34 upregulated) proportion of genes showed > 2 fold (P-value of 0.05, FDR of 0.05) change in their expression, while only 23 genes down-regulated by >2 fold. Furthermore, no transcripts for potential allergenic proteins were represented in the DEGs. Most of these genes appeared to be developmentally regulated or stress-related which was expected because absolute synchronous growth and development even under a controlled environment are challenging. A few upregulated (AT-hook motif nuclear-localized protein 17-like, probable inactive 2-oxoglutaratedependent dioxygenase AOP2, protein EXORDIUM-like) and down-regulated (histone H2B, gonadal, embryonic abundant protein VF30.1-like, fasciclin-like arabinogalactan protein 12) genes were subjected to qPCR. The qPCR data validated the fold change of the up-regulated (>2) and down-regulated (>-2) genes. Thus, the above data revealed no potential alterations in the nutritional equivalence or transcript profile of transgenic Bt chickpeas.
  • Thumbnail Image
    ThesisItemOpen Access
    Molecular characterization and nutritional equivalence evaluation of transgenic chickpea expressing either a cry1Ac or cry2Aa gen
    (AAU, Jorhat, 2019-10) Gupta, Rubi; Sarmah, Bidyut Kumar
    iosafety assessment of transgenic chickpeas having B.thuringiensis genes for resistance to pod borers is a regulatory requirement and mandatory to document before releasing in the field. Therefore, Bt chickpea lines harbouring either a cry1Ac or cry2Aa gene were characterized for the presence and expression of the transgene in their advanced generations, biosafety assessments and transcript profile were studied. The homozygous lines were selected for comparative nutritional equivalence assay. Biochemical estimations of major nutritional components such as proximates, vitamins, minerals, fatty acids and anti nutrients confirmed that the Bt chickpeas lines are nutritionally equivalent to their non-transgenic counterparts and the seed composition is similar or within the range reported, previously. Seed protein quality was investigated by separating the proteins in PAGE and eluted proteins after mass spectrometry (MS) showed expected fractions of 11S legumin, 7S vicilin, and 2S albumin of chickpea storage proteins in the transgenic lines. The protein digestibility was assayed using the multi-enzyme system and transient pepsin hydrolysis to mimic simulated gastric fluid followed by trypsin hydrolysis to mimic simulated intestinal fluid. Total seed proteins of both the transgenic and nontransgenic lines were digested at a similar rate and enzyme-resistant peptides were not observed in transgenic Bt chickpea lines. The unintended changes in the whole transcriptome profile of Bt chickpeas were surveyed using a homozygous transgenic line expressing a cry1Ac gene. The differentially expressed genes (DEGs) profiling confirmed a low (0.69%, log2fold change≥2) frequency of differentially expressed in the transgenic chickpea line. Only a small (34 upregulated) proportion of genes showed > 2 fold (P-value of 0.05, FDR of 0.05) change in their expression, while only 23 genes down-regulated by >2 fold. Furthermore, no transcripts for potential allergenic proteins were represented in the DEGs. Most of these genes appeared to be developmentally regulated or stress-related which was expected because absolute synchronous growth and development even under a controlled environment are challenging. A few upregulated (AT-hook motif nuclear-localized protein 17-like, probable inactive 2-oxoglutaratedependent dioxygenase AOP2, protein EXORDIUM-like) and down-regulated (histone H2B, gonadal, embryonic abundant protein VF30.1-like, fasciclin-like arabinogalactan protein 12) genes were subjected to qPCR. The qPCR data validated the fold change of the up-regulated (>2) and down-regulated (>-2) genes. Thus, the above data revealed no potential alterations in the nutritional equivalence or transcript profile of transgenic Bt chickpeas.