Immobilization of His-tagged recombinant xylanase from Penicillium occitanis on nickel-chelate Eupergit C for increasing digestibility of poultry feed.
Identifieur interne : 000052 ( PubMed/Corpus ); précédent : 000051; suivant : 000053Immobilization of His-tagged recombinant xylanase from Penicillium occitanis on nickel-chelate Eupergit C for increasing digestibility of poultry feed.
Auteurs : Dorra Driss ; Zied Driss ; Fatma Chaari ; Semia Ellouz ChaabouniSource :
- Bioengineered [ 2165-5987 ]
English descriptors
- KwdEn :
- MESH :
- chemical , biosynthesis : Glucuronates, Oligosaccharides.
- chemical , metabolism : Endo-1,4-beta Xylanases, Fungal Proteins.
- enzymology : Penicillium.
Abstract
Recombinant xylanase 2 from Penicillium occitanis expressed with an 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. Thermodynamically, increase in enthalpy and free energy change after covalent immobilization could be credited to the enhanced stability. Immobilized xylanase could be reused for 10 consecutive cycles retaining 60% of its initial activity. It was found to be effective in releasing reducing sugar from poultry feed. Immobilization on Eupergit C is important due to its mechanical resistance at high pH and temperature. Hence, considerable stability and reusability of bound enzyme may be advantageous for its industrial application.
DOI: 10.4161/bioe.29596
PubMed: 24932488
Links to Exploration step
pubmed:24932488Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Immobilization of His-tagged recombinant xylanase from Penicillium occitanis on nickel-chelate Eupergit C for increasing digestibility of poultry feed.</title><author><name sortKey="Driss, Dorra" sort="Driss, Dorra" uniqKey="Driss D" first="Dorra" last="Driss">Dorra Driss</name><affiliation><nlm:affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author><author><name sortKey="Driss, Zied" sort="Driss, Zied" uniqKey="Driss Z" first="Zied" last="Driss">Zied Driss</name><affiliation><nlm:affiliation>Laboratory of Electro-Mechanic Systems (LASEM); National Engineering School of Sfax (ENIS); University of Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author><author><name sortKey="Chaari, Fatma" sort="Chaari, Fatma" uniqKey="Chaari F" first="Fatma" last="Chaari">Fatma Chaari</name><affiliation><nlm:affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author><author><name sortKey="Chaabouni, Semia Ellouz" sort="Chaabouni, Semia Ellouz" uniqKey="Chaabouni S" first="Semia Ellouz" last="Chaabouni">Semia Ellouz Chaabouni</name><affiliation><nlm:affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia; Unité de service commun bioréacteur couplé à un ultrafiltre; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>2014 Jul-Aug</MedlineDate></PubDate></date><idno type="RBID">pubmed:24932488</idno><idno type="pmid">24932488</idno><idno type="doi">10.4161/bioe.29596</idno><idno type="wicri:Area/PubMed/Corpus">000052</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000052</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Immobilization of His-tagged recombinant xylanase from Penicillium occitanis on nickel-chelate Eupergit C for increasing digestibility of poultry feed.</title><author><name sortKey="Driss, Dorra" sort="Driss, Dorra" uniqKey="Driss D" first="Dorra" last="Driss">Dorra Driss</name><affiliation><nlm:affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author><author><name sortKey="Driss, Zied" sort="Driss, Zied" uniqKey="Driss Z" first="Zied" last="Driss">Zied Driss</name><affiliation><nlm:affiliation>Laboratory of Electro-Mechanic Systems (LASEM); National Engineering School of Sfax (ENIS); University of Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author><author><name sortKey="Chaari, Fatma" sort="Chaari, Fatma" uniqKey="Chaari F" first="Fatma" last="Chaari">Fatma Chaari</name><affiliation><nlm:affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author><author><name sortKey="Chaabouni, Semia Ellouz" sort="Chaabouni, Semia Ellouz" uniqKey="Chaabouni S" first="Semia Ellouz" last="Chaabouni">Semia Ellouz Chaabouni</name><affiliation><nlm:affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia; Unité de service commun bioréacteur couplé à un ultrafiltre; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Bioengineered</title><idno type="eISSN">2165-5987</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Endo-1,4-beta Xylanases (metabolism)</term><term>Fungal Proteins (metabolism)</term><term>Glucuronates (biosynthesis)</term><term>Oligosaccharides (biosynthesis)</term><term>Penicillium (enzymology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Glucuronates</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Penicillium</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recombinant xylanase 2 from Penicillium occitanis expressed with an 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. Thermodynamically, increase in enthalpy and free energy change after covalent immobilization could be credited to the enhanced stability. Immobilized xylanase could be reused for 10 consecutive cycles retaining 60% of its initial activity. It was found to be effective in releasing reducing sugar from poultry feed. Immobilization on Eupergit C is important due to its mechanical resistance at high pH and temperature. Hence, considerable stability and reusability of bound enzyme may be advantageous for its industrial application.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24932488</PMID><DateCreated><Year>2014</Year><Month>08</Month><Day>15</Day></DateCreated><DateCompleted><Year>2015</Year><Month>05</Month><Day>12</Day></DateCompleted><DateRevised><Year>2015</Year><Month>08</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2165-5987</ISSN><JournalIssue CitedMedium="Internet"><Volume>5</Volume><Issue>4</Issue><PubDate><MedlineDate>2014 Jul-Aug</MedlineDate></PubDate></JournalIssue><Title>Bioengineered</Title><ISOAbbreviation>Bioengineered</ISOAbbreviation></Journal><ArticleTitle>Immobilization of His-tagged recombinant xylanase from Penicillium occitanis on nickel-chelate Eupergit C for increasing digestibility of poultry feed.</ArticleTitle><Pagination><MedlinePgn>274-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4161/bioe.29596</ELocationID><Abstract><AbstractText>Recombinant xylanase 2 from Penicillium occitanis expressed with an 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. Thermodynamically, increase in enthalpy and free energy change after covalent immobilization could be credited to the enhanced stability. Immobilized xylanase could be reused for 10 consecutive cycles retaining 60% of its initial activity. It was found to be effective in releasing reducing sugar from poultry feed. Immobilization on Eupergit C is important due to its mechanical resistance at high pH and temperature. Hence, considerable stability and reusability of bound enzyme may be advantageous for its industrial application.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Driss</LastName><ForeName>Dorra</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Driss</LastName><ForeName>Zied</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Laboratory of Electro-Mechanic Systems (LASEM); National Engineering School of Sfax (ENIS); University of Sfax; Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chaari</LastName><ForeName>Fatma</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chaabouni</LastName><ForeName>Semia Ellouz</ForeName><Initials>SE</Initials><AffiliationInfo><Affiliation>Unité Enzymes et Bioconversion; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia; Unité de service commun bioréacteur couplé à un ultrafiltre; Ecole Nationale d'Ingénieurs de Sfax; Université de Sfax; Sfax, Tunisia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016420">Comment</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>06</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Bioengineered</MedlineTA><NlmUniqueID>101581063</NlmUniqueID><ISSNLinking>2165-5979</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005965">Glucuronates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber><NameOfSubstance UI="D043364">Endo-1,4-beta Xylanases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Biosci Biotechnol Biochem. 2001 Mar;65(3):527-33</RefSource><PMID Version="1">11330664</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Appl Biochem Biotechnol. 2014 Jul;173(6):1405-18</RefSource><PMID Version="1">24801404</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biotechnol Bioeng. 2001 Aug 5;74(3):249-55</RefSource><PMID Version="1">11400098</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biotechnol Bioeng. 2001 Nov;76(3):269-76</RefSource><PMID Version="1">11668463</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biochem Biophys Methods. 2001 Oct 30;49(1-3):313-34</RefSource><PMID Version="1">11694287</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Microbiol Res. 2002;157(4):275-81</RefSource><PMID Version="1">12501991</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biomacromolecules. 2003 Jan-Feb;4(1):107-13</RefSource><PMID Version="1">12523854</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Chromatogr A. 2003 Feb 21;988(1):1-23</RefSource><PMID Version="1">12647817</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Microbiol Rev. 1988 Sep;52(3):305-17</RefSource><PMID Version="1">3141761</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biotechnol Appl Biochem. 1995 Apr;21 ( Pt 2):217-22</RefSource><PMID Version="1">7718159</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Crit Rev Biotechnol. 1997;17(1):39-67</RefSource><PMID Version="1">9118232</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biotechnol. 1998 Feb 5;60(1-2):37-46</RefSource><PMID Version="1">9571800</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biotechnol. 1998 Dec 11;66(2-3):165-75</RefSource><PMID Version="1">9866868</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Br Poult Sci. 2007 Aug;48(4):480-8</RefSource><PMID Version="1">17701501</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Agric Food Chem. 2009 Jan 14;57(1):109-15</RefSource><PMID Version="1">19061308</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Protein Expr Purif. 2012 May;83(1):8-14</RefSource><PMID Version="1">22402470</PMID></CommentsCorrections><CommentsCorrections RefType="CommentOn"><RefSource>Appl Biochem Biotechnol. 2014 Jul;173(6):1405-18</RefSource><PMID Version="1">24801404</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D043364" MajorTopicYN="N">Endo-1,4-beta Xylanases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005965" MajorTopicYN="N">Glucuronates</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009844" MajorTopicYN="N">Oligosaccharides</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010407" MajorTopicYN="N">Penicillium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4143399</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Ni-Eupergit C</Keyword><Keyword MajorTopicYN="N">Penicillium occitanis</Keyword><Keyword MajorTopicYN="N">immobilization</Keyword><Keyword MajorTopicYN="N">poultry feed</Keyword><Keyword MajorTopicYN="N">thermodynamic</Keyword><Keyword MajorTopicYN="N">xylanase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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