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  <Article>
    <Journal>
      <PublisherName>emergentresearch</PublisherName>
      <JournalTitle>Emergent Life Sciences Research</JournalTitle>
      <PISSN>2395-6658 (</PISSN>
      <EISSN>) 2395-664X (Print)</EISSN>
      <Volume-Issue>Vol 9, Issue 1, Published on 30</Volume-Issue>
      <PartNumber/>
      <IssueTopic>Multidisciplinary</IssueTopic>
      <IssueLanguage>English</IssueLanguage>
      <Season>June 2023</Season>
      <SpecialIssue>N</SpecialIssue>
      <SupplementaryIssue>N</SupplementaryIssue>
      <IssueOA>Y</IssueOA>
      <PubDate>
        <Year>-0001</Year>
        <Month>11</Month>
        <Day>30</Day>
      </PubDate>
      <ArticleType>Research Article</ArticleType>
      <ArticleTitle>Production, partial purification and characterization of intracellular Azoreductase from bacterial isolates during biodecolorization of textile dye Acid Maroon V</ArticleTitle>
      <SubTitle/>
      <ArticleLanguage>English</ArticleLanguage>
      <ArticleOA>Y</ArticleOA>
      <FirstPage>61</FirstPage>
      <LastPage>71</LastPage>
      <AuthorList>
        <Author>
          <FirstName>Yogesh</FirstName>
          <LastName>Patel</LastName>
          <AuthorLanguage>English</AuthorLanguage>
          <Affiliation/>
          <CorrespondingAuthor>N</CorrespondingAuthor>
          <ORCID/>
          <FirstName>Akshaya</FirstName>
          <LastName>Gupte</LastName>
          <AuthorLanguage>English</AuthorLanguage>
          <Affiliation/>
          <CorrespondingAuthor>Y</CorrespondingAuthor>
          <ORCID/>
        </Author>
      </AuthorList>
      <DOI/>
      <Abstract>Azoreductase is an important enzyme for the reduction of the azo linkage of dye during the biodecolorization process. In the present study, the production of intracellular azoreductase from bacterial cultures Enterobacter dissolvens AGYP1 (ED) and Pseudomonas aeruginosa AGYP2 (PA) was achieved during biodecolorization of synthetic textile dye Acid Maroon V. When compared with PA, the enzyme activity of ED was 2.31 times greater. The partial purification of azoreductase revealed specific activity of the dialyzed enzyme 51.72 U mg-1 protein (ED) and 33.06 U mg-1 protein (PA). Methyl Red served as the best substrate for the azoreductase enzyme with superior activity at optimal pH 7 and temperature 30 __degreesignC. 75-80% of azoreductase enzyme activity was maintained when Mg+2 and Ca+2 were present. The azoreductase activity was considerably increased with NADH as the most suitable electron donor. The kinetic study showed consequent Michaelis-Menten constant (Km) and maximal velocity (Vmax) values of 50 __ampersandsignmu;M and 2222 U ml-1 (ED) and 250 __ampersandsignmu;M and 1000 U ml-1 (PA), respectively.</Abstract>
      <AbstractLanguage>English</AbstractLanguage>
      <Keywords>azoreductase, bacterial cultures ED and PA, characterization, decolorization</Keywords>
      <URLs>
        <Abstract>https://emergentresearch.org/ubijournal-v1copy/journals/abstract.php?article_id=14360&amp;title=Production, partial purification and characterization of intracellular Azoreductase from bacterial isolates during biodecolorization of textile dye Acid Maroon V</Abstract>
      </URLs>
      <References>
        <ReferencesarticleTitle>References</ReferencesarticleTitle>
        <ReferencesfirstPage>16</ReferencesfirstPage>
        <ReferenceslastPage>19</ReferenceslastPage>
        <References/>
      </References>
    </Journal>
  </Article>
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