Purification and characterisation of κ-casein specific milk-clotting metalloprotease from Termitomyces clypeatus MTCC 5091.
Identifieur interne : 001B72 ( Main/Exploration ); précédent : 001B71; suivant : 001B73Purification and characterisation of κ-casein specific milk-clotting metalloprotease from Termitomyces clypeatus MTCC 5091.
Auteurs : Rajib Majumder [Inde] ; Samudra Prosad Banik [Inde] ; Suman Khowala [Inde]Source :
- Food chemistry [ 1873-7072 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Aspartic acid endopeptidases (MeSH), Caséines (métabolisme), Chymosine (métabolisme), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Fromage (MeSH), Hydrolyse (MeSH), Lait (métabolisme), Metalloproteases (composition chimique), Metalloproteases (isolement et purification), Metalloproteases (métabolisme), Température (MeSH), Termitomyces (enzymologie).
- MESH :
- composition chimique : Metalloproteases.
- enzymologie : Termitomyces.
- isolement et purification : Metalloproteases.
- métabolisme : Caséines, Chymosine, Lait, Metalloproteases.
- Animaux, Aspartic acid endopeptidases, Cinétique, Concentration en ions d'hydrogène, Fromage, Hydrolyse, Température.
English descriptors
- KwdEn :
- Animals (MeSH), Aspartic Acid Endopeptidases (MeSH), Caseins (metabolism), Cheese (MeSH), Chymosin (metabolism), Hydrogen-Ion Concentration (MeSH), Hydrolysis (MeSH), Kinetics (MeSH), Metalloproteases (chemistry), Metalloproteases (isolation & purification), Metalloproteases (metabolism), Milk (metabolism), Temperature (MeSH), Termitomyces (enzymology).
- MESH :
- chemical , chemistry : Metalloproteases.
- chemical , isolation & purification : Metalloproteases.
- chemical , metabolism : Caseins, Chymosin, Metalloproteases.
- chemical : Aspartic Acid Endopeptidases.
- enzymology : Termitomyces.
- metabolism : Milk.
- Animals, Cheese, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Temperature.
Abstract
Milk-clotting enzymes are valued as chymosin-like protease substitutes for cheese making industries. An extracellular metalloprotease (AcPs) with high milk-clotting activity was purified from edible mushroom Termitomyces clypeatus and characterised. AcPs was preferentially active towards κ-casein, analysed by Urea-PAGE and LC-ESI-MS, whereas the degradation of α and β-casein components by AcPs proceeded slowly justifying its suitability for cheese making. RP-HPLC peptide profiling revealed that the AcPs activity on milk casein was similar to that of a commercial milk coagulant. The enzyme exhibited pH and temperature optima at 5.0 and 45 °C, respectively and showed a pI value of 4.6. One- and two dimensional zymographies revealed a single polypeptide band with proteolytic signal. The MALDI-TOF/MS followed by peptide mass fingerprinting revealed homology with a predicted protein of Populus trichocarpa. To our knowledge, this is the first report on a metalloprotease from T. clypeatus, and the results indicate that this enzyme can be considered as a potential substitute for chymosin in cheese manufacturing.
DOI: 10.1016/j.foodchem.2014.10.027
PubMed: 25466043
Affiliations:
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Mullick Road, Kolkata 700032, West Bengal</wicri:regionArea><wicri:noRegion>West Bengal</wicri:noRegion></affiliation></author></analytic><series><title level="j">Food chemistry</title><idno type="eISSN">1873-7072</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Aspartic Acid Endopeptidases (MeSH)</term><term>Caseins (metabolism)</term><term>Cheese (MeSH)</term><term>Chymosin (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Hydrolysis (MeSH)</term><term>Kinetics (MeSH)</term><term>Metalloproteases (chemistry)</term><term>Metalloproteases (isolation & purification)</term><term>Metalloproteases (metabolism)</term><term>Milk (metabolism)</term><term>Temperature (MeSH)</term><term>Termitomyces (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Aspartic acid endopeptidases (MeSH)</term><term>Caséines (métabolisme)</term><term>Chymosine (métabolisme)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Fromage (MeSH)</term><term>Hydrolyse (MeSH)</term><term>Lait (métabolisme)</term><term>Metalloproteases (composition chimique)</term><term>Metalloproteases (isolement et purification)</term><term>Metalloproteases (métabolisme)</term><term>Température (MeSH)</term><term>Termitomyces (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Metalloproteases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Metalloproteases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Caseins</term><term>Chymosin</term><term>Metalloproteases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Aspartic Acid Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Metalloproteases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Termitomyces</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Termitomyces</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Metalloproteases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Milk</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Caséines</term><term>Chymosine</term><term>Lait</term><term>Metalloproteases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cheese</term><term>Hydrogen-Ion Concentration</term><term>Hydrolysis</term><term>Kinetics</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Aspartic acid endopeptidases</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Fromage</term><term>Hydrolyse</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Milk-clotting enzymes are valued as chymosin-like protease substitutes for cheese making industries. An extracellular metalloprotease (AcPs) with high milk-clotting activity was purified from edible mushroom Termitomyces clypeatus and characterised. AcPs was preferentially active towards κ-casein, analysed by Urea-PAGE and LC-ESI-MS, whereas the degradation of α and β-casein components by AcPs proceeded slowly justifying its suitability for cheese making. RP-HPLC peptide profiling revealed that the AcPs activity on milk casein was similar to that of a commercial milk coagulant. The enzyme exhibited pH and temperature optima at 5.0 and 45 °C, respectively and showed a pI value of 4.6. One- and two dimensional zymographies revealed a single polypeptide band with proteolytic signal. The MALDI-TOF/MS followed by peptide mass fingerprinting revealed homology with a predicted protein of Populus trichocarpa. To our knowledge, this is the first report on a metalloprotease from T. clypeatus, and the results indicate that this enzyme can be considered as a potential substitute for chymosin in cheese manufacturing.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">25466043</PMID><DateCompleted><Year>2015</Year><Month>07</Month><Day>24</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-7072</ISSN><JournalIssue CitedMedium="Internet"><Volume>173</Volume><PubDate><Year>2015</Year><Month>Apr</Month><Day>15</Day></PubDate></JournalIssue><Title>Food chemistry</Title><ISOAbbreviation>Food Chem</ISOAbbreviation></Journal><ArticleTitle>Purification and characterisation of κ-casein specific milk-clotting metalloprotease from Termitomyces clypeatus MTCC 5091.</ArticleTitle><Pagination><MedlinePgn>441-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.foodchem.2014.10.027</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0308-8146(14)01589-1</ELocationID><Abstract><AbstractText>Milk-clotting enzymes are valued as chymosin-like protease substitutes for cheese making industries. An extracellular metalloprotease (AcPs) with high milk-clotting activity was purified from edible mushroom Termitomyces clypeatus and characterised. AcPs was preferentially active towards κ-casein, analysed by Urea-PAGE and LC-ESI-MS, whereas the degradation of α and β-casein components by AcPs proceeded slowly justifying its suitability for cheese making. RP-HPLC peptide profiling revealed that the AcPs activity on milk casein was similar to that of a commercial milk coagulant. The enzyme exhibited pH and temperature optima at 5.0 and 45 °C, respectively and showed a pI value of 4.6. One- and two dimensional zymographies revealed a single polypeptide band with proteolytic signal. The MALDI-TOF/MS followed by peptide mass fingerprinting revealed homology with a predicted protein of Populus trichocarpa. To our knowledge, this is the first report on a metalloprotease from T. clypeatus, and the results indicate that this enzyme can be considered as a potential substitute for chymosin in cheese manufacturing.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Majumder</LastName><ForeName>Rajib</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Drug Development Diagnostics and Biotechnology Division, CSIR-Indian Institute of Chemical Biology, 4, Raja S.C. Mullick Road, Kolkata 700032, West Bengal, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Banik</LastName><ForeName>Samudra Prosad</ForeName><Initials>SP</Initials><AffiliationInfo><Affiliation>Maulana Azad College, Department of Microbiology, 8, Rafi Ahmed Kidwai Road, Kolkata 700013, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Khowala</LastName><ForeName>Suman</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Drug Development Diagnostics and Biotechnology Division, CSIR-Indian Institute of Chemical Biology, 4, Raja S.C. Mullick Road, Kolkata 700032, West Bengal, India. Electronic address: sumankhowala@iicb.res.in.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Food Chem</MedlineTA><NlmUniqueID>7702639</NlmUniqueID><ISSNLinking>0308-8146</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002364">Caseins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D045726">Metalloproteases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.-</RegistryNumber><NameOfSubstance UI="D016282">Aspartic Acid Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.-</RegistryNumber><NameOfSubstance UI="C022517">rennin-like enzyme (Aspergillus ochraceus)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.4</RegistryNumber><NameOfSubstance UI="D012085">Chymosin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016282" MajorTopicYN="N">Aspartic Acid Endopeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002364" MajorTopicYN="N">Caseins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002611" MajorTopicYN="N">Cheese</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012085" MajorTopicYN="N">Chymosin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045726" MajorTopicYN="N">Metalloproteases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008892" MajorTopicYN="N">Milk</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055434" MajorTopicYN="N">Termitomyces</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Edible mushroom</Keyword><Keyword MajorTopicYN="N">Metalloprotease</Keyword><Keyword MajorTopicYN="N">Milk clotting activity</Keyword><Keyword MajorTopicYN="N">Peptide mass fingerprinting</Keyword><Keyword MajorTopicYN="N">Termitomyces clypeatus</Keyword><Keyword MajorTopicYN="N">Urea-PAGE</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>09</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>10</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>12</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>12</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>7</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25466043</ArticleId><ArticleId IdType="pii">S0308-8146(14)01589-1</ArticleId><ArticleId IdType="doi">10.1016/j.foodchem.2014.10.027</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Majumder, Rajib" sort="Majumder, Rajib" uniqKey="Majumder R" first="Rajib" last="Majumder">Rajib Majumder</name></noRegion><name sortKey="Banik, Samudra Prosad" sort="Banik, Samudra Prosad" uniqKey="Banik S" first="Samudra Prosad" last="Banik">Samudra Prosad Banik</name><name sortKey="Khowala, Suman" sort="Khowala, Suman" uniqKey="Khowala S" first="Suman" last="Khowala">Suman Khowala</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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