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<records>

  <record>
    <language>eng</language>
          <publisher>Oriental Scientific Publishing Company</publisher>
        <journalTitle>Biosciences Biotechnology Research Asia</journalTitle>
          <issn>0973-1245</issn>
            <publicationDate>2017-06-28</publicationDate>
    
        <volume>14</volume>
        <issue>2</issue>

 
    <startPage>503</startPage>
    <endPage>507</endPage>

	 
      <doi>10.13005/bbra/2471</doi>
        <publisherRecordId>25808</publisherRecordId>
    <documentType>article</documentType>
    <title language="eng">Cloning and Characterization of Lipase Gene from A Local Isolate of Pseudoxanthomonas Sp.</title>

    <authors>
	 


      <author>
       <name>Yogi Yopa Kristia</name>

 
		
	<affiliationId>1</affiliationId>
      </author>
    

	 


      <author>
       <name>Syifa F Syihab</name>


		
	<affiliationId>1</affiliationId>

      </author>
    

	 


      <author>
       <name>Akhmaloka`</name>

		
	<affiliationId>1,2</affiliationId>
      </author>
    

	


	


	
    </authors>
    
	    <affiliationsList>
	    
		
		<affiliationName affiliationId="1">Biochemistry Research Group, Faculty of Mathematics and Natural Sciences. Institut Teknologi Bandung, Jl. Ganesha no. 10 Bandung 40132, Indonesia.</affiliationName>
    

		
		<affiliationName affiliationId="2">Departement of Chemistry, Faculty of Sciences and Computer. Universitas Pertamina, Jakarta, Indonesia.</affiliationName>
    
		
		
		
		
	  </affiliationsList>






    <abstract language="eng">Lipase gene from <em>Pseudoxanthomonas </em>sp. was cloned through <em>in vitro </em>amplification from total chromosomal DNA. The gene was sequenced and characterized, coding for 312 amino acid residues. Homological analysis showed that the gene has 98% similarity to lipolytic gene from <em>Uncultured Pseudomonas </em>sp (GenBank No. AKA58891.1). Further analysis appeared that the sequences showed similar unique motifs of lipase sub-family I.1, such as pentapeptide (GHSHG) motif, tetrapeptide (GMLG) motif, and catalytic triad. In additional, 3D structure analysis based on crystal structure of <em>Pseudomonas aeruginose</em> (PDB ID 1ex9) showed that both structure of lipases are similar except on the conformation of catalytic residue of His<sup>277</sup> showing to shift more far away compared to that the control.</abstract>

    <fullTextUrl format="html">https://www.biotech-asia.org/vol14no2/cloning-and-characterization-of-lipase-gene-from-a-local-isolate-of-pseudoxanthomonas-sp/</fullTextUrl>



      <keywords language="eng">
        <keyword><em>Cloning; Sequencing; Characterization P. seudoxanthomonas </em>sp<em>.</em>; Thermostable lipase;</keyword>
      </keywords>

  </record>
</records>