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	<ArticleSet>

	<Article> 

	<Journal> 

	<PublisherName>International Science Community Association</PublisherName>

	<JournalTitle>International Research Journal of Biological Sciences</JournalTitle> 

	<Issn>2278 - 3202</Issn>

	<Volume>6</Volume>

	<Issue>1</Issue>

	<PubDate PubStatus="ppublish"> 

	<Year>2017</Year> 

	<Month>01</Month> 

	<Day>10</Day> 

	</PubDate>

	</Journal>



	<ArticleTitle>Synthesize a transfer vector containing the gene encoding ADP-glucose pyrophosphorylase enzyme to improve the starch content in Manihot esculenta Crantz</ArticleTitle> 


	<FirstPage>25</FirstPage>

	<LastPage>33</LastPage>



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	<Language>EN</Language> 
	<AuthorList>

	
		<Author> 

		<FirstName>Dawane</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Vinars </LastName>

		<Suffix>1</Suffix>

		<Affiliation>School of Environment and Sustainable Development, Central University of Gujarat, Gandhinagar – 382030, Gandhinagar, Gujarat, India</Affiliation>

		</Author>
		<Author> 

		<FirstName>Fulekar </FirstName>

		<MiddleName> </MiddleName>

		<LastName>M.H. </LastName>

		<Suffix>2</Suffix>

		<Affiliation>School of Environment and Sustainable Development, Central University of Gujarat, Gandhinagar – 382030, Gandhinagar, Gujarat, India</Affiliation>

		</Author>
		<Author> 

		<FirstName>Dieudonne</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Mutangana </LastName>

		<Suffix>1</Suffix>

		<Affiliation>University of Rwanda, College of Science and Technology, Department of Biology, Avenue de l’Armée, Po. Box 3900, Kigali-Rwanda</Affiliation>

		</Author>
		<Author> 

		<FirstName>Innocent</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Uwintwali </LastName>

		<Suffix>2</Suffix>

		<Affiliation>University of Rwanda, College of Science and Technology, Department of Biology, Avenue de l’Armée, Po. Box 3900, Kigali-Rwanda</Affiliation>

		</Author>
		<Author> 

		<FirstName>Eug&#1104;ne </FirstName>

		<MiddleName> </MiddleName>

		<LastName>Ndisanze M. </LastName>

		<Suffix>3</Suffix>

		<Affiliation>University of Rwanda, College of Science and Technology, Department of Biology, Avenue de l’Armée, Po. Box 3900, Kigali-Rwanda</Affiliation>

		</Author>
		<Author> 

		<FirstName>Mahurpawar </FirstName>

		<MiddleName> </MiddleName>

		<LastName>Manju </LastName>

		<Suffix>1</Suffix>

		<Affiliation>Dept. of Zoology, Govt P.G. College, Parasia (Chhindwara) M.P., India</Affiliation>

		</Author>
		<Author> 

		<FirstName>Khatoon</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Akhtari </LastName>

		<Suffix>1</Suffix>

		<Affiliation>P.G. Department of Botany, Utkal University, Vani Vihar, Bhubaneswar-751004, Odisha, India</Affiliation>

		</Author>
		<Author> 

		<FirstName>Mohapatra</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Ashirbad </LastName>

		<Suffix>2</Suffix>

		<Affiliation>Sri Jayadev College of Education and Technology, Naharkanta, Bhubaneswar-752101, Odisha, India</Affiliation>

		</Author>
		<Author> 

		<FirstName>Satapathy </FirstName>

		<MiddleName> </MiddleName>

		<LastName>Kunja Bihari </LastName>

		<Suffix>3</Suffix>

		<Affiliation>P.G. Department of Botany, Utkal University, Vani Vihar, Bhubaneswar-751004, Odisha, India</Affiliation>

		</Author>
		<Author> 

		<FirstName>Lan</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Do Hai </LastName>

		<Suffix>1</Suffix>

		<Affiliation>Faculty of Biology - Chemistry, Tay Bac University, Quyet Tam, District - S&#417;n La City, Vietnam</Affiliation>

		</Author>
		<Author> 

		<FirstName>Son</FirstName>

		<MiddleName> </MiddleName>

		<LastName>Le Van </LastName>

		<Suffix>2</Suffix>

		<Affiliation>Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Vietnam</Affiliation>

		</Author>
		<Author> 

		<FirstName>Binh </FirstName>

		<MiddleName> </MiddleName>

		<LastName>Le Tran </LastName>

		<Suffix>3</Suffix>

		<Affiliation>Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Vietnam</Affiliation>

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	<CollectiveName></CollectiveName>>

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	<PublicationType>Research Paper</PublicationType>


	<History>  
	<PubDate PubStatus="received">
	<Year>2016</Year>
	<Month>12</Month>
	<Day>18</Day>
	</PubDate>
	<PubDate PubStatus="accepted">										
	<Year>2017</Year> 
	<Month>01</Month>									
	<Day>10</Day> 
	</PubDate>

	</History>
	<Abstract>Starch is polysaccharide which plays important role in the metabolism of living organisms. In addition, starch is raw materials in the food and materials industry. Increasing the starch content of crops based on improving the activity of some genes encoding enzymes plays an important role in the process of biosynthesis and accumulation of starch, which is one of the research are of interest. Like in bacteria, the process of starch biosynthesis in plants occurs by using ADP-Glc as raw materials to made long link chain &</Abstract>

	<CopyrightInformation>Copyright@ International Science Community Association</CopyrightInformation>

	<ObjectList> 
	<Object Type="keyword">
	<Param Name="value">945;-1.4-glucoside. ADP-Glcpyrophosphorylase (AGPase) has an important role in the biosynthesis of ADP-Glc molecule</Param>
	</Object><Object Type="keyword">
	<Param Name="value"> and therefore AGPase is a critical enzyme of glycogen synthesis in bacteria and starch in plants. In this study</Param>
	</Object><Object Type="keyword">
	<Param Name="value"> the gene encoding for AGPase enzyme (symbol Lan1_opt)</Param>
	</Object><Object Type="keyword">
	<Param Name="value"> size 1.5 kb originating from the glgC gene coding for the enzyme AGPase of E. coli has been optimised. This gene had G336 mutation replacing aspartic acid by glycin in order to decrease the affinity of the inhibitor. It has been combined with gene transfer plant vector and was transformed into tobacco plants</Param>
	</Object><Object Type="keyword">
	<Param Name="value"> operated under the control of a 35S promoter. The integration of the Lan1_opt gene into plant genome was confirmed by PCR technique showing the expression of AGPase proteins in the genomic tobacco plants. Moreover</Param>
	</Object><Object Type="keyword">
	<Param Name="value"> AGPase enzyme activity in leaves of this genomic tobacco plants was higher than 21%-43% compared with the AGPase enzyme activity in leaves of tobacco plants control. Our data provided the gene encoding AGPase (Lan1_opt) was an effective strategy to strength the process of starch biosynthesis in plants.</Param>
	</Object>

	</ObjectList>	

	</Article>

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