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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>2016-05-07</publicationDate>
    
        <volume>9</volume>
        <issue>2</issue>

 
    <startPage></startPage>
    <endPage></endPage>

	 
      <doi>http://dx.doi.org/10.13005/bbra/1034</doi>
        <publisherRecordId>9932</publisherRecordId>
    <documentType>article</documentType>
    <title language="eng">Characterization of Immobilized L-Asparaginase Produced from Pseudomonas aeruginosa 50071 by Solid State Fermentation</title>

    <authors>
	 


      <author>
       <name>Mohsen M. S. Asker</name>

 
		
	<affiliationId>1</affiliationId>
      </author>
    

	 


      <author>
       <name>Sahera F. Mohamed</name>


		
	<affiliationId>1.2</affiliationId>

      </author>
    

	 


      <author>
       <name>Osama H. El-sayed</name>

		
	<affiliationId>2</affiliationId>
      </author>
    

	


	


	
    </authors>
    
	    <affiliationsList>
	    
		
		<affiliationName affiliationId="1">Microbial Biotechnology Department, National Research Center, Dokki, Cairo, Egypt.</affiliationName>
    

		
		<affiliationName affiliationId="2">Chemistry Department, College of Science, Jazan University, Jazan, KSA.</affiliationName>
    
		
		
		
		
	  </affiliationsList>






    <abstract language="eng">The natural polymer sodium alginate is a macropolysaccharide Produced from brown algae has many applications. Anti-leukemia enzyme L-asparaginase (L-ASNase) produced from Pseudomonas aeruginosa 50071 by solid state fermentation was covalently conjugated on sodium alginate. SDS-PAGE showed that the purified L-ASNase was homogeneous with molecular weight of ~ 113 KDa. The immobilized enzyme on 3% sodium alginate showed specific activity of 62 U/mg protein. The immobilized L-ASNase maintained over 90 % of the original activity of free enzyme. Also it showed a slightly thermal stability where the activation energy of denaturation were 28 and 35 Kcal mol-1 for both native and immobilized enzyme, respectively. The Km of sodium alginate immobilized enzyme was about 2 times lower than that of the free enzyme.</abstract>

    <fullTextUrl format="html">https://www.biotech-asia.org/vol9no2/characterization-of-immobilized-l-asparaginase-produced-from-pseudomonas-aeruginosa-50071-by-solid-state-fermentation/</fullTextUrl>



      <keywords language="eng">
        <keyword><p class="normal-font">Immobilization; L-asparaginase; pseudomonas aeruginosa; solid state fermentation.</p></keyword>
      </keywords>

  </record>
</records>