Production and structure prediction of amylases from Chlorella vulgaris.
Identifieur interne : 000020 ( Main/Exploration ); précédent : 000019; suivant : 000021Production and structure prediction of amylases from Chlorella vulgaris.
Auteurs : Hajer Ben Hlima [Tunisie] ; Aida Karray [Tunisie] ; Mouna Dammak [Tunisie] ; Fatma Elleuch [Tunisie] ; Philippe Michaud [France] ; Imen Fendri [Tunisie] ; Slim Abdelkafi [Tunisie]Source :
- Environmental science and pollution research international [ 1614-7499 ] ; 2021.
Abstract
Amylases are enzymes required for starch degradation and are naturally produced by many microorganisms. These enzymes are used in several fields such as food processing, beverage, and medicine as well as in the formulation of enzymatic detergents proving their significance in modern biotechnology. In this study, a three-stage growth mode was applied to enhance starch production and amylase detection from Chlorella vulgaris. Stress conditions applied in the second stage of cultivation led to an accumulation of proteins (75% DW) and starch (21% DW) and a decrease in biomass. Amylase activities were detected and they showed high production levels especially on day 3 (35 U/ml) and day 5 (22.5 U/ml) of the second and third stages, respectively. The bioinformatic tools used to seek amylase protein sequences from TSA database of C. vulgaris revealed 7 putative genes encoding for 4 α-amylases, 2 β-amylases, and 1 isoamylase. An in silico investigation showed that these proteins are different in their lengths as well as in their cellular localizations and oligomeric states though they share common features like CSRs of GH13 family or active site of GH14 family. In brief, this study allowed for the production and in silico characterization of amylases from C. vulgaris.
DOI: 10.1007/s11356-021-14357-9
PubMed: 33973124
Affiliations:
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Biochimie et de Génie Enzymatique des Lipases, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3018, Sfax, Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3018, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author><author><name sortKey="Dammak, Mouna" sort="Dammak, Mouna" uniqKey="Dammak M" first="Mouna" last="Dammak">Mouna Dammak</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, 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des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author><author><name sortKey="Karray, Aida" sort="Karray, Aida" uniqKey="Karray A" first="Aida" last="Karray">Aida Karray</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3018, Sfax, Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3018, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author><author><name sortKey="Dammak, Mouna" sort="Dammak, Mouna" uniqKey="Dammak M" first="Mouna" last="Dammak">Mouna Dammak</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author><author><name sortKey="Elleuch, Fatma" sort="Elleuch, Fatma" uniqKey="Elleuch F" first="Fatma" last="Elleuch">Fatma Elleuch</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author><author><name sortKey="Michaud, Philippe" sort="Michaud, Philippe" uniqKey="Michaud P" first="Philippe" last="Michaud">Philippe Michaud</name><affiliation wicri:level="3"><nlm:affiliation>Université Clermont Auvergne, CNRS, SIGMA Clermont, Institut Pascal, F-63000, Clermont-Ferrand, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université Clermont Auvergne, CNRS, SIGMA Clermont, Institut Pascal, F-63000, Clermont-Ferrand</wicri:regionArea><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Auvergne (région administrative)</region><settlement type="city">Clermont-Ferrand</settlement></placeName></affiliation></author><author><name sortKey="Fendri, Imen" sort="Fendri, Imen" uniqKey="Fendri I" first="Imen" last="Fendri">Imen Fendri</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Biotechnologie des Plantes Appliquée à l'Amélioration des Plantes Faculté des Sciences de Sfax, Université de Sfax, Sfax, Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire de Biotechnologie des Plantes Appliquée à l'Amélioration des Plantes Faculté des Sciences de Sfax, Université de Sfax, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author><author><name sortKey="Abdelkafi, Slim" sort="Abdelkafi, Slim" uniqKey="Abdelkafi S" first="Slim" last="Abdelkafi">Slim Abdelkafi</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia. slim.abdelkafi@enis.tn.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author></analytic><series><title level="j">Environmental science and pollution research international</title><idno type="eISSN">1614-7499</idno><imprint><date when="2021" type="published">2021</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Amylases are enzymes required for starch degradation and are naturally produced by many microorganisms. These enzymes are used in several fields such as food processing, beverage, and medicine as well as in the formulation of enzymatic detergents proving their significance in modern biotechnology. In this study, a three-stage growth mode was applied to enhance starch production and amylase detection from Chlorella vulgaris. Stress conditions applied in the second stage of cultivation led to an accumulation of proteins (75% DW) and starch (21% DW) and a decrease in biomass. Amylase activities were detected and they showed high production levels especially on day 3 (35 U/ml) and day 5 (22.5 U/ml) of the second and third stages, respectively. The bioinformatic tools used to seek amylase protein sequences from TSA database of C. vulgaris revealed 7 putative genes encoding for 4 α-amylases, 2 β-amylases, and 1 isoamylase. An in silico investigation showed that these proteins are different in their lengths as well as in their cellular localizations and oligomeric states though they share common features like CSRs of GH13 family or active site of GH14 family. In brief, this study allowed for the production and in silico characterization of amylases from C. vulgaris.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33973124</PMID><DateRevised><Year>2021</Year><Month>05</Month><Day>11</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1614-7499</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2021</Year><Month>May</Month><Day>11</Day></PubDate></JournalIssue><Title>Environmental science and pollution research international</Title><ISOAbbreviation>Environ Sci Pollut Res Int</ISOAbbreviation></Journal><ArticleTitle>Production and structure prediction of amylases from Chlorella vulgaris.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11356-021-14357-9</ELocationID><Abstract><AbstractText>Amylases are enzymes required for starch degradation and are naturally produced by many microorganisms. These enzymes are used in several fields such as food processing, beverage, and medicine as well as in the formulation of enzymatic detergents proving their significance in modern biotechnology. In this study, a three-stage growth mode was applied to enhance starch production and amylase detection from Chlorella vulgaris. Stress conditions applied in the second stage of cultivation led to an accumulation of proteins (75% DW) and starch (21% DW) and a decrease in biomass. Amylase activities were detected and they showed high production levels especially on day 3 (35 U/ml) and day 5 (22.5 U/ml) of the second and third stages, respectively. The bioinformatic tools used to seek amylase protein sequences from TSA database of C. vulgaris revealed 7 putative genes encoding for 4 α-amylases, 2 β-amylases, and 1 isoamylase. An in silico investigation showed that these proteins are different in their lengths as well as in their cellular localizations and oligomeric states though they share common features like CSRs of GH13 family or active site of GH14 family. In brief, this study allowed for the production and in silico characterization of amylases from C. vulgaris.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ben Hlima</LastName><ForeName>Hajer</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Karray</LastName><ForeName>Aida</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3018, Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dammak</LastName><ForeName>Mouna</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Elleuch</LastName><ForeName>Fatma</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Michaud</LastName><ForeName>Philippe</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Université Clermont Auvergne, CNRS, SIGMA Clermont, Institut Pascal, F-63000, Clermont-Ferrand, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fendri</LastName><ForeName>Imen</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Laboratoire de Biotechnologie des Plantes Appliquée à l'Amélioration des Plantes Faculté des Sciences de Sfax, Université de Sfax, Sfax, Tunisia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Abdelkafi</LastName><ForeName>Slim</ForeName><Initials>S</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-1314-0523</Identifier><AffiliationInfo><Affiliation>Laboratoire de Génie Enzymatique et de Microbiologie, Equipe de Biotechnologie des Algues, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, 3038, Sfax, Tunisia. slim.abdelkafi@enis.tn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2021</Year><Month>05</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Environ Sci Pollut Res Int</MedlineTA><NlmUniqueID>9441769</NlmUniqueID><ISSNLinking>0944-1344</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Bioinformatic tools</Keyword><Keyword MajorTopicYN="N">Culture mode</Keyword><Keyword MajorTopicYN="N">Enzymes</Keyword><Keyword MajorTopicYN="N">Glycoside hydrolase</Keyword><Keyword MajorTopicYN="N">Microalgae</Keyword><Keyword MajorTopicYN="N">Molecular modeling</Keyword><Keyword MajorTopicYN="N">Starch</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2021</Year><Month>01</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2021</Year><Month>05</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2021</Year><Month>5</Month><Day>11</Day><Hour>6</Hour><Minute>42</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2021</Year><Month>5</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2021</Year><Month>5</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33973124</ArticleId><ArticleId IdType="doi">10.1007/s11356-021-14357-9</ArticleId><ArticleId IdType="pii">10.1007/s11356-021-14357-9</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Abdelkafi S, Chamkha M, Casalot L, Sayadi S, Labat M (2005) Isolation and characterization of a novel Bacillus sp., strain YAS1, capable of transforming tyrosol under hypersaline conditions. 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