Sensitivity of the Bacillus subtilis Xyn A Xylanase and Its Mutants to Different Xylanase Inhibitors Determines Their Activity Profile and Functionality during Bread Making.
Identifieur interne : 000029 ( Main/Exploration ); précédent : 000028; suivant : 000030Sensitivity of the Bacillus subtilis Xyn A Xylanase and Its Mutants to Different Xylanase Inhibitors Determines Their Activity Profile and Functionality during Bread Making.
Auteurs : Sofie Leys [Belgique] ; Yamina De Bondt [Belgique] ; Linde Schreurs [Belgique] ; Christophe M. Courtin [Belgique]Source :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2019.
Descripteurs français
- KwdFr :
- Antienzymes (composition chimique), Antienzymes (métabolisme), Bacillus subtilis (composition chimique), Bacillus subtilis (enzymologie), Bacillus subtilis (génétique), Endo-1,4-beta xylanases (antagonistes et inhibiteurs), Endo-1,4-beta xylanases (composition chimique), Endo-1,4-beta xylanases (génétique), Endo-1,4-beta xylanases (métabolisme), Farine (analyse), Hydrolyse (MeSH), Manipulation des aliments (MeSH), Mutation (MeSH), Pain (analyse), Protéines bactériennes (antagonistes et inhibiteurs), Protéines bactériennes (composition chimique), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (métabolisme), Triticum (composition chimique), Triticum (métabolisme), Viscosité (MeSH).
- MESH :
- analyse : Farine, Pain.
- antagonistes et inhibiteurs : Endo-1,4-beta xylanases, Protéines bactériennes.
- composition chimique : Antienzymes, Bacillus subtilis, Endo-1,4-beta xylanases, Protéines bactériennes, Protéines végétales, Triticum.
- enzymologie : Bacillus subtilis.
- génétique : Bacillus subtilis, Endo-1,4-beta xylanases, Protéines bactériennes.
- métabolisme : Antienzymes, Endo-1,4-beta xylanases, Protéines bactériennes, Protéines végétales, Triticum.
- Hydrolyse, Manipulation des aliments, Mutation, Viscosité.
English descriptors
- KwdEn :
- Bacillus subtilis (chemistry), Bacillus subtilis (enzymology), Bacillus subtilis (genetics), Bacterial Proteins (antagonists & inhibitors), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Bread (analysis), Endo-1,4-beta Xylanases (antagonists & inhibitors), Endo-1,4-beta Xylanases (chemistry), Endo-1,4-beta Xylanases (genetics), Endo-1,4-beta Xylanases (metabolism), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (metabolism), Flour (analysis), Food Handling (MeSH), Hydrolysis (MeSH), Mutation (MeSH), Plant Proteins (chemistry), Plant Proteins (metabolism), Triticum (chemistry), Triticum (metabolism), Viscosity (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Bacterial Proteins, Endo-1,4-beta Xylanases.
- analysis : Bread, Flour.
- chemistry : Bacillus subtilis, Bacterial Proteins, Endo-1,4-beta Xylanases, Enzyme Inhibitors, Plant Proteins, Triticum.
- enzymology : Bacillus subtilis.
- genetics : Bacillus subtilis, Bacterial Proteins, Endo-1,4-beta Xylanases.
- chemical , metabolism : Bacterial Proteins, Endo-1,4-beta Xylanases, Enzyme Inhibitors, Plant Proteins, Triticum.
- Food Handling, Hydrolysis, Mutation, Viscosity.
Abstract
The importance of inhibition sensitivity for xylanase functionality in bread making was investigated using mutants of the wild-type Bacillus subtilis xylanase (XBSTAXI), sensitive to Triticum aestivum xylanase inhibitor (TAXI). XBSNI, a mutant with reduced sensitivity to TAXI, and XBSTI, a mutant sensitive to all wheat endogenous proteinaceous inhibitors (TAXI, Xylanase Inhibiting Protein and Thaumatin-like Xylanase Inhibitor) were used. The higher inhibition sensitivity of XBSTAXI and XBSTI compared to XBSNI was associated with a respective 7- and 53-fold increase in enzyme dosage required for a maximal increase in bread loaf volume. XBSTI and XBSTAXI were only active during the mixing phase and the beginning of fermentation, while XBSNI was able to hydrolyze arabinoxylan until the end of fermentation. In spite of this difference in activity profile, no differences in loaf volume were observed for the different xylanases at optimal concentrations. Dough extensional viscosity analysis suggests that increased water availability as a result of xylanase activity favors starch-starch and starch-gluten interactions and drives the improvement in bread loaf volume.
DOI: 10.1021/acs.jafc.9b04712
PubMed: 31532988
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xylanases</term><term>Protéines bactériennes</term><term>Protéines végétales</term><term>Triticum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Food Handling</term><term>Hydrolysis</term><term>Mutation</term><term>Viscosity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Hydrolyse</term><term>Manipulation des aliments</term><term>Mutation</term><term>Viscosité</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The importance of inhibition sensitivity for xylanase functionality in bread making was investigated using mutants of the wild-type <i>Bacillus subtilis</i> xylanase (XBS<sub>TAXI</sub>), sensitive to <i>Triticum aestivum</i> xylanase inhibitor (TAXI). XBS<sub>NI</sub>, a mutant with reduced sensitivity to TAXI, and XBS<sub>TI</sub>, a mutant sensitive to all wheat endogenous proteinaceous inhibitors (TAXI, Xylanase Inhibiting Protein and Thaumatin-like Xylanase Inhibitor) were used. The higher inhibition sensitivity of XBS<sub>TAXI</sub> and XBS<sub>TI</sub> compared to XBS<sub>NI</sub> was associated with a respective 7- and 53-fold increase in enzyme dosage required for a maximal increase in bread loaf volume. XBS<sub>TI</sub> and XBS<sub>TAXI</sub> were only active during the mixing phase and the beginning of fermentation, while XBS<sub>NI</sub> was able to hydrolyze arabinoxylan until the end of fermentation. In spite of this difference in activity profile, no differences in loaf volume were observed for the different xylanases at optimal concentrations. Dough extensional viscosity analysis suggests that increased water availability as a result of xylanase activity favors starch-starch and starch-gluten interactions and drives the improvement in bread loaf volume.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31532988</PMID><DateCompleted><Year>2019</Year><Month>10</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5118</ISSN><JournalIssue CitedMedium="Internet"><Volume>67</Volume><Issue>40</Issue><PubDate><Year>2019</Year><Month>Oct</Month><Day>09</Day></PubDate></JournalIssue><Title>Journal of agricultural and food chemistry</Title><ISOAbbreviation>J Agric Food Chem</ISOAbbreviation></Journal><ArticleTitle>Sensitivity of the <i>Bacillus subtilis</i> Xyn A Xylanase and Its Mutants to Different Xylanase Inhibitors Determines Their Activity Profile and Functionality during Bread Making.</ArticleTitle><Pagination><MedlinePgn>11198-11209</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.jafc.9b04712</ELocationID><Abstract><AbstractText>The importance of inhibition sensitivity for xylanase functionality in bread making was investigated using mutants of the wild-type <i>Bacillus subtilis</i> xylanase (XBS<sub>TAXI</sub>), sensitive to <i>Triticum aestivum</i> xylanase inhibitor (TAXI). XBS<sub>NI</sub>, a mutant with reduced sensitivity to TAXI, and XBS<sub>TI</sub>, a mutant sensitive to all wheat endogenous proteinaceous inhibitors (TAXI, Xylanase Inhibiting Protein and Thaumatin-like Xylanase Inhibitor) were used. The higher inhibition sensitivity of XBS<sub>TAXI</sub> and XBS<sub>TI</sub> compared to XBS<sub>NI</sub> was associated with a respective 7- and 53-fold increase in enzyme dosage required for a maximal increase in bread loaf volume. XBS<sub>TI</sub> and XBS<sub>TAXI</sub> were only active during the mixing phase and the beginning of fermentation, while XBS<sub>NI</sub> was able to hydrolyze arabinoxylan until the end of fermentation. In spite of this difference in activity profile, no differences in loaf volume were observed for the different xylanases at optimal concentrations. Dough extensional viscosity analysis suggests that increased water availability as a result of xylanase activity favors starch-starch and starch-gluten interactions and drives the improvement in bread loaf volume.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Leys</LastName><ForeName>Sofie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre (LFoRCe) , KU Leuven , Kasteelpark Arenberg 20 , 3001 Leuven , Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>De Bondt</LastName><ForeName>Yamina</ForeName><Initials>Y</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-6043-7800</Identifier><AffiliationInfo><Affiliation>Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre (LFoRCe) , KU Leuven , Kasteelpark Arenberg 20 , 3001 Leuven , Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schreurs</LastName><ForeName>Linde</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre (LFoRCe) , KU Leuven , Kasteelpark Arenberg 20 , 3001 Leuven , Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Courtin</LastName><ForeName>Christophe M</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre (LFoRCe) , KU Leuven , Kasteelpark Arenberg 20 , 3001 Leuven , Belgium.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>09</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Agric Food Chem</MedlineTA><NlmUniqueID>0374755</NlmUniqueID><ISSNLinking>0021-8561</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber><NameOfSubstance UI="D043364">Endo-1,4-beta Xylanases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001412" MajorTopicYN="N">Bacillus subtilis</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001939" MajorTopicYN="N">Bread</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043364" MajorTopicYN="N">Endo-1,4-beta Xylanases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005433" MajorTopicYN="N">Flour</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005511" MajorTopicYN="N">Food Handling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014908" MajorTopicYN="N">Triticum</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014783" MajorTopicYN="N">Viscosity</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">arabinoxylan</Keyword><Keyword MajorTopicYN="N">bread making</Keyword><Keyword MajorTopicYN="N">dough rheology</Keyword><Keyword MajorTopicYN="N">enzyme</Keyword><Keyword MajorTopicYN="N">inhibition sensitivity</Keyword><Keyword MajorTopicYN="N">wheat</Keyword><Keyword MajorTopicYN="N">xylanase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>10</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31532988</ArticleId><ArticleId IdType="doi">10.1021/acs.jafc.9b04712</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Belgique</li></country><region><li>Province du Brabant flamand</li></region><settlement><li>Heverlee</li><li>Louvain</li></settlement></list><tree><country name="Belgique"><region name="Province du Brabant flamand"><name sortKey="Leys, Sofie" sort="Leys, Sofie" uniqKey="Leys S" first="Sofie" last="Leys">Sofie Leys</name></region><name sortKey="Courtin, Christophe M" sort="Courtin, Christophe M" uniqKey="Courtin C" first="Christophe M" last="Courtin">Christophe M. Courtin</name><name sortKey="De Bondt, Yamina" sort="De Bondt, Yamina" uniqKey="De Bondt Y" first="Yamina" last="De Bondt">Yamina De Bondt</name><name sortKey="Schreurs, Linde" sort="Schreurs, Linde" uniqKey="Schreurs L" first="Linde" last="Schreurs">Linde Schreurs</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Sensitivity of the Bacillus subtilis Xyn A Xylanase and Its Mutants to Different Xylanase Inhibitors Determines Their Activity Profile and Functionality during Bread Making.
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