<?xml version='1.0' encoding='UTF-8'?>
<modsCollection xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-3.xsd" xmlns="http://www.loc.gov/mods/v3" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"><mods><titleInfo><title>Hydroxytyrosol from tyrosol using hydroxyphenylacetic acid-induced bacterial cultures and evidence of the role of 4-HPA 3-hydroxylase</title></titleInfo><name type="personal"><namePart type="family">Liebgott</namePart><namePart type="given">P-P.</namePart><role><roleTerm type="text">auteur</roleTerm><roleTerm type="code" authority="marcrelator">aut</roleTerm></role></name><name type="personal"><namePart type="family">Amouric</namePart><namePart type="given">A.</namePart><role><roleTerm type="text">auteur</roleTerm><roleTerm type="code" authority="marcrelator">aut</roleTerm></role></name><name type="personal"><namePart type="family">Comte</namePart><namePart type="given">A.</namePart><role><roleTerm type="text">auteur</roleTerm><roleTerm type="code" authority="marcrelator">aut</roleTerm></role></name><name type="personal"><namePart type="family">Tholozan</namePart><namePart type="given">Jean-Luc</namePart><role><roleTerm type="text">auteur</roleTerm><roleTerm type="code" authority="marcrelator">aut</roleTerm></role></name><name type="personal"><namePart type="family">Lorquin</namePart><namePart type="given">Jean</namePart><role><roleTerm type="text">auteur</roleTerm><roleTerm type="code" authority="marcrelator">aut</roleTerm></role><affiliation>IRD</affiliation></name><typeOfResource>text</typeOfResource><genre authority="local">journalArticle</genre><physicalDescription><internetMediaType>text/pdf</internetMediaType><digitalOrigin>born digital</digitalOrigin><reformattingQuality>access</reformattingQuality></physicalDescription><abstract>Hydroxytyrosol (HTyr) is a potent natural antioxidant found in olive mill wastewaters. Bacterial conversion of 4-tyrosol (2-(4-hydroxyphenyl)-ethanol) to HTyr was reported in a limited number of bacterial species including Pseudomonas aeruginosa. In this work, we studied this conversion, taking as a model the newly isolated Halomonas sp. strain HTB24. It was first hypothesized that the enzyme responsible for 4-tyrosol hydroxylation in HTyr was a 4-hydroxyphenylacetic acid 3-hydroxylase (HPAH, EC 1.14.13.3), previously known to convert 4-hydroxyphenylacetic acid (4-HPA) into 3,4-dihydroxyphenylacetic acid (3,4-DHPA) in P. aeruginosa. Cloning and expression of hpaB (oxygenase component) and hpaC (reductase component) genes from P. aeruginosa confirmed this hypothesis. Furthermore, using cultures of HTB24 containing 4-tyrosol, it was shown that 4-HPA accumulation preceded 4-tyrosol hydroxylation. We further demonstrated that the synthesis of HPAH activity was induced by 4-HPA, with the latter compound being formed from 4-tyrosol oxidation by aryl-dehydrogenases. Interestingly, similar results were obtained with other 4-HPA-induced bacteria, including P. aeruginosa, Serratia marcescens, Escherichia coli, Micrococcus luteus and other Halomonas, thus demonstrating general hydroxylating activity of 4-tyrosol by the HPAH enzyme. E. coli W did not have aryl-dehydrogenase activity and hence were unable to oxidize 4-tyrosol to 4-HPA and HTyr to 3,4-DHPA, making this bacterium a good candidate for achieving better HTyr production.</abstract><targetAudience authority="marctarget">specialized</targetAudience><subject><topic>Hydroxytyrosol</topic><topic>Tyrosol</topic><topic>Induction</topic><topic>4-hydroxyphenylacetic acid</topic><topic>4-HPA</topic><topic>3-hydroxylase</topic></subject><classification authority="local">084 </classification><relatedItem type="host"><titleInfo><title>Research in Microbiology</title></titleInfo><part><detail type="volume"><number>160</number></detail><detail type="issue"><number>10</number></detail><extent unit="pages"><start>757</start><end>766</end></extent></part><originInfo><dateIssued>2009</dateIssued></originInfo><identifier type="issn">0923-2508</identifier></relatedItem><identifier type="uri">http://www.documentation.ird.fr/hor/fdi:010049099</identifier><identifier type="doi">10.1016/j.resmic.2009.09.015</identifier><location><physicalLocation>IRD Bondy</physicalLocation><shelfLocator>F B010049099</shelfLocator><url usage="primary display" access="object in context">http://www.documentation.ird.fr/hor/fdi:010049099</url><url access="raw object">http://www.documentation.ird.fr/intranet/publi/2010/01/010049099.pdf</url></location><accessCondition type="restriction on access" displayLabel="Accès réservé">Accès réservé (Intranet de l'IRD)</accessCondition><recordInfo><recordContentSource>IRD - Base Horizon / Pleins textes</recordContentSource><recordCreationDate encoding="w3cdtf">2010-02-08</recordCreationDate><recordChangeDate encoding="w3cdtf">2010-02-08</recordChangeDate><recordIdentifier>fdi:010049099</recordIdentifier><languageOfCataloging><languageTerm authority="iso639-2b">fre</languageTerm></languageOfCataloging></recordInfo></mods></modsCollection>