Production of xylooligosaccharides by immobilized His-tagged recombinant xylanase from Penicillium occitanis on nickel-chelate Eupergit C.
Identifieur interne : 000023 ( France/Analysis ); précédent : 000022; suivant : 000024Production of xylooligosaccharides by immobilized His-tagged recombinant xylanase from Penicillium occitanis on nickel-chelate Eupergit C.
Auteurs : Dorra Driss [France] ; Anissa Haddar ; Raoudha Ghorbel ; Semia Ellouz ChaabouniSource :
- Applied biochemistry and biotechnology [ 1559-0291 ] ; 2014.
English descriptors
- KwdEn :
- Biotechnology, Chelating Agents, Disaccharides (biosynthesis), Endo-1,4-beta Xylanases (metabolism), Enzyme Stability, Enzymes, Immobilized (genetics), Enzymes, Immobilized (metabolism), Fermentation, Fungal Proteins (genetics), Fungal Proteins (metabolism), Glucuronates (biosynthesis), Glucuronates (chemistry), Hydrogen-Ion Concentration, Hydrolysis, Nickel, Oligosaccharides (biosynthesis), Oligosaccharides (chemistry), Penicillium (enzymology), Penicillium (genetics), Pichia (enzymology), Pichia (genetics), Polymers, Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Temperature, Trisaccharides (biosynthesis), Xylans (metabolism), Zea mays.
- MESH :
- chemical , biosynthesis : Disaccharides, Glucuronates, Oligosaccharides, Trisaccharides.
- chemical , chemistry : Glucuronates, Oligosaccharides.
- chemical , genetics : Enzymes, Immobilized, Fungal Proteins, Recombinant Proteins.
- chemical , metabolism : Endo-1,4-beta Xylanases, Enzymes, Immobilized, Fungal Proteins, Recombinant Proteins, Xylans.
- chemical : Chelating Agents, Nickel, Polymers.
- enzymology : Penicillium, Pichia.
- genetics : Penicillium, Pichia.
- Biotechnology, Enzyme Stability, Fermentation, Hydrogen-Ion Concentration, Hydrolysis, Temperature, Zea mays.
Abstract
Penicillium occitanis xylanase 2 expressed with a His-tag in Pichia pastoris, termed PoXyn2, was immobilized on nickel-chelate Eupergit C by covalent coupling reaction with a high immobilization yield up to 93.49 %. Characterization of the immobilized PoXyn2 was further evaluated. The optimum pH was not affected by immobilization, but the immobilized PoXyn2 exhibited more acidic and large optimum pH range (pH 2.0-4.0) than that of the free PoXyn2 (pH 3.0). The free PoXyn2 had an optimum temperature of 50 °C, whereas that of the immobilized enzyme was shifted to 65 °C. Immobilization increased both pH stability and thermostability when compared with the free enzyme. Time courses of the xylooligosaccharides (XOS) produced from corncob xylan indicated that the immobilized enzyme tends to use shorter xylan chains and to produce more xylobiose and xylotriose initially. At the end of 24-h reaction, XOS mixture contained a total of 21.3 and 34.2 % (w/w) of xylobiose and xylotriose with immobilized xylanase and free xylanase, respectively. The resulting XOS could be used as a special nutrient for lactic bacteria.
DOI: 10.1007/s12010-014-0932-0
PubMed: 24801404
Affiliations:
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pubmed:24801404Le document en format XML
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Haddar</name></author><author><name sortKey="Ghorbel, Raoudha" sort="Ghorbel, Raoudha" uniqKey="Ghorbel R" first="Raoudha" last="Ghorbel">Raoudha Ghorbel</name></author><author><name sortKey="Chaabouni, Semia Ellouz" sort="Chaabouni, Semia Ellouz" uniqKey="Chaabouni S" first="Semia Ellouz" last="Chaabouni">Semia Ellouz Chaabouni</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24801404</idno><idno type="pmid">24801404</idno><idno type="doi">10.1007/s12010-014-0932-0</idno><idno type="wicri:Area/PubMed/Corpus">000051</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000051</idno><idno type="wicri:Area/PubMed/Curation">000051</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000051</idno><idno type="wicri:Area/PubMed/Checkpoint">000051</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" 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wicri:rule="url">France</country><wicri:regionArea>Unité Enzymes et Bioconversion, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, route de Soukra, 3038, Sfax, Tunisia</wicri:regionArea><wicri:noRegion>Tunisia</wicri:noRegion><wicri:noRegion>Tunisia</wicri:noRegion></affiliation></author><author><name sortKey="Haddar, Anissa" sort="Haddar, Anissa" uniqKey="Haddar A" first="Anissa" last="Haddar">Anissa Haddar</name></author><author><name sortKey="Ghorbel, Raoudha" sort="Ghorbel, Raoudha" uniqKey="Ghorbel R" first="Raoudha" last="Ghorbel">Raoudha Ghorbel</name></author><author><name sortKey="Chaabouni, Semia Ellouz" sort="Chaabouni, Semia Ellouz" uniqKey="Chaabouni S" first="Semia Ellouz" last="Chaabouni">Semia Ellouz Chaabouni</name></author></analytic><series><title level="j">Applied biochemistry and biotechnology</title><idno type="eISSN">1559-0291</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biotechnology</term><term>Chelating Agents</term><term>Disaccharides (biosynthesis)</term><term>Endo-1,4-beta Xylanases (metabolism)</term><term>Enzyme Stability</term><term>Enzymes, Immobilized (genetics)</term><term>Enzymes, Immobilized (metabolism)</term><term>Fermentation</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Glucuronates (biosynthesis)</term><term>Glucuronates (chemistry)</term><term>Hydrogen-Ion Concentration</term><term>Hydrolysis</term><term>Nickel</term><term>Oligosaccharides (biosynthesis)</term><term>Oligosaccharides (chemistry)</term><term>Penicillium (enzymology)</term><term>Penicillium (genetics)</term><term>Pichia (enzymology)</term><term>Pichia (genetics)</term><term>Polymers</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Temperature</term><term>Trisaccharides (biosynthesis)</term><term>Xylans (metabolism)</term><term>Zea mays</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Disaccharides</term><term>Glucuronates</term><term>Oligosaccharides</term><term>Trisaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glucuronates</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Enzymes, Immobilized</term><term>Fungal Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Enzymes, Immobilized</term><term>Fungal Proteins</term><term>Recombinant Proteins</term><term>Xylans</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Chelating Agents</term><term>Nickel</term><term>Polymers</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Penicillium</term><term>Pichia</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Penicillium</term><term>Pichia</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biotechnology</term><term>Enzyme Stability</term><term>Fermentation</term><term>Hydrogen-Ion Concentration</term><term>Hydrolysis</term><term>Temperature</term><term>Zea mays</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Penicillium occitanis xylanase 2 expressed with a His-tag in Pichia pastoris, termed PoXyn2, was immobilized on nickel-chelate Eupergit C by covalent coupling reaction with a high immobilization yield up to 93.49 %. Characterization of the immobilized PoXyn2 was further evaluated. The optimum pH was not affected by immobilization, but the immobilized PoXyn2 exhibited more acidic and large optimum pH range (pH 2.0-4.0) than that of the free PoXyn2 (pH 3.0). The free PoXyn2 had an optimum temperature of 50 °C, whereas that of the immobilized enzyme was shifted to 65 °C. Immobilization increased both pH stability and thermostability when compared with the free enzyme. Time courses of the xylooligosaccharides (XOS) produced from corncob xylan indicated that the immobilized enzyme tends to use shorter xylan chains and to produce more xylobiose and xylotriose initially. At the end of 24-h reaction, XOS mixture contained a total of 21.3 and 34.2 % (w/w) of xylobiose and xylotriose with immobilized xylanase and free xylanase, respectively. The resulting XOS could be used as a special nutrient for lactic bacteria.</div></front></TEI><affiliations><list><country><li>France</li></country></list><tree><noCountry><name sortKey="Chaabouni, Semia Ellouz" sort="Chaabouni, Semia Ellouz" uniqKey="Chaabouni S" first="Semia Ellouz" last="Chaabouni">Semia Ellouz Chaabouni</name><name sortKey="Ghorbel, Raoudha" sort="Ghorbel, Raoudha" uniqKey="Ghorbel R" first="Raoudha" last="Ghorbel">Raoudha Ghorbel</name><name sortKey="Haddar, Anissa" sort="Haddar, Anissa" uniqKey="Haddar A" first="Anissa" last="Haddar">Anissa Haddar</name></noCountry><country name="France"><noRegion><name sortKey="Driss, Dorra" sort="Driss, Dorra" uniqKey="Driss D" first="Dorra" last="Driss">Dorra Driss</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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