<?xml version="1.0" encoding="UTF-8"?>



<records>

  <record>
    <language>eng</language>
          <publisher>Oriental Scientific Publishing Company</publisher>
        <journalTitle>Biosciences Biotechnology Research Asia</journalTitle>
          <issn>0973-1245</issn>
            <publicationDate>2016-04-27</publicationDate>
    
        <volume>6</volume>
        <issue>2</issue>

 
    <startPage>489</startPage>
    <endPage>496</endPage>

	    <publisherRecordId>8639</publisherRecordId>
    <documentType>article</documentType>
    <title language="eng">Inhibition of Mushroom Tyrosinase by Aliphatic Alcholols</title>

    <authors>
	 


      <author>
       <name>R. Sariri</name>

 
		
	<affiliationId>1</affiliationId>
      </author>
    

	 


      <author>
       <name>F. Aghaghaziani </name>


		
	<affiliationId>1</affiliationId>

      </author>
    

	 


      <author>
       <name>R. Hassan Sajedi</name>

		
	<affiliationId>1</affiliationId>
      </author>
    

	


	


	
    </authors>
    
	    <affiliationsList>
	    
		
		<affiliationName affiliationId="1">Department of Biology, Faculty of Science, University of Guilan, Rasht (Iran).</affiliationName>
    

		
		
		
		
		
	  </affiliationsList>






    <abstract language="eng">Browning of fruits and vegetables damaged by mechanical injury during harvesting, postharvest storage or processing is one of the main causes of quality loss. Tyrosinase catalyzes the oxidation of phenolic compounds to the corresponding quinines and is responsible for the enzymatic browning of fruits and vegetables. Although the use of compounds such as organic acids, amines and thiols as tyrosinase inhibitors have been studied and reported, but alcohols have received less attention in this regard. This paper reports inhibition of polyphenol oxidase activity by aliphatic alcohols using dopamine hydrochloride as substrate. It was observed that hydroxy containing compounds inhibited tyrosinase activity by a revesible mixed-noncompetitive mechanism. Many kinetic constants, such as Vmax, Kcat and Ki were also obtained in each case.</abstract>

    <fullTextUrl format="html">https://www.biotech-asia.org/vol6no2/inhibition-of-mushroom-tyrosinase-by-aliphatic-alcholols/</fullTextUrl>



      <keywords language="eng">
        <keyword>Tyrosinase; inhibition; enzyme kinetics; alcoholic inhibitors</keyword>
      </keywords>

  </record>
</records>