Purification, characterization and antibacterial potential of a lectin isolated from Apuleia leiocarpa seeds
Apuleia leiocarpa is a tree found in Caatinga that has great value in the timber industry. Lectins are carbohydrate-binding proteins with several biotechnological applications. This study shows the isolation, characterization, and antibacterial activity of A. leiocarpa seed lectin (ApulSL). The lect...
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| Veröffentlicht in: | International journal of biological macromolecules 2015-04, Vol.75, p.402-408 |
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| creator | Carvalho, Aline de Souza da Silva, Márcia Vanusa Gomes, Francis Soares Paiva, Patrícia Maria Guedes Malafaia, Carolina Barbosa da Silva, Tulio Diego Vaz, Antônio Fernando de Melo da Silva, Alexandre Gomes Arruda, Isabel Renata de Souza Napoleão, Thiago Henrique Carneiro-da-Cunha, Maria das Graças Correia, Maria Tereza dos Santos |
| description | Apuleia leiocarpa is a tree found in Caatinga that has great value in the timber industry. Lectins are carbohydrate-binding proteins with several biotechnological applications. This study shows the isolation, characterization, and antibacterial activity of A. leiocarpa seed lectin (ApulSL). The lectin was chromatographically isolated from a crude extract (in 150mM NaCl) by using a chitin column. ApulSL adsorbed to the matrix and was eluted using 1.0M acetic acid. Native ApulSL was characterized as a 55.8-kDa acidic protein. SDS-PAGE showed three polypeptide bands, whereas two-dimensional electrophoresis revealed four spots. The peptides detected by MALDI TOF/TOF did not show sufficient homology ( |
| doi_str_mv | 10.1016/j.ijbiomac.2015.02.001 |
| format | Article |
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Lectins are carbohydrate-binding proteins with several biotechnological applications. This study shows the isolation, characterization, and antibacterial activity of A. leiocarpa seed lectin (ApulSL). The lectin was chromatographically isolated from a crude extract (in 150mM NaCl) by using a chitin column. ApulSL adsorbed to the matrix and was eluted using 1.0M acetic acid. Native ApulSL was characterized as a 55.8-kDa acidic protein. SDS-PAGE showed three polypeptide bands, whereas two-dimensional electrophoresis revealed four spots. The peptides detected by MALDI TOF/TOF did not show sufficient homology (<30%) with the database proteins. Circular dichroism spectroscopy suggested a disordered conformational structure, and fluorescence spectrum showed the presence of tyrosine residues in the hydrophobic core. The hemagglutinating activity of ApulSL was present even after heating to 100°C, was Mn2+-dependent, and inhibited by N-acetylglucosamine, d(−)-arabinose, and azocasein. ApulSL demonstrated bacteriostatic and bactericide effects on gram-positive and gram-negative species, being more effective against three varieties of Xanthomonas campestris (MIC ranging from 11.2 to 22.5μg/mL and MBC of 22.5μg/mL). The results of this study reinforce the importance of biochemical prospecting of Caatinga by revealing the antibacterial potential of ApulSL.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2015.02.001</identifier><identifier>PMID: 25668321</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Apuleia leiocarpa ; Bacteria - drug effects ; Chromatography, Gel ; Electrophoresis, Gel, Two-Dimensional ; Fabaceae - chemistry ; Hemagglutination - drug effects ; Hemagglutinins - chemistry ; Humans ; Lectin ; Mass Spectrometry ; Microbial Sensitivity Tests ; Peptides - chemistry ; Plant Lectins - chemistry ; Plant Lectins - isolation & purification ; Plant Lectins - pharmacology ; Rabbits ; Seeds - chemistry ; Xanthomonas campestris</subject><ispartof>International journal of biological macromolecules, 2015-04, Vol.75, p.402-408</ispartof><rights>2015 Elsevier B.V.</rights><rights>Copyright © 2015 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-873bafcb4da18681d53f905164d7f91b36bf3cc3315ddbee4b24f2fea4a955293</citedby><cites>FETCH-LOGICAL-c368t-873bafcb4da18681d53f905164d7f91b36bf3cc3315ddbee4b24f2fea4a955293</cites><orcidid>0000-0002-0065-2602</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2015.02.001$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25668321$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carvalho, Aline de Souza</creatorcontrib><creatorcontrib>da Silva, Márcia Vanusa</creatorcontrib><creatorcontrib>Gomes, Francis Soares</creatorcontrib><creatorcontrib>Paiva, Patrícia Maria Guedes</creatorcontrib><creatorcontrib>Malafaia, Carolina Barbosa</creatorcontrib><creatorcontrib>da Silva, Tulio Diego</creatorcontrib><creatorcontrib>Vaz, Antônio Fernando de Melo</creatorcontrib><creatorcontrib>da Silva, Alexandre Gomes</creatorcontrib><creatorcontrib>Arruda, Isabel Renata de Souza</creatorcontrib><creatorcontrib>Napoleão, Thiago Henrique</creatorcontrib><creatorcontrib>Carneiro-da-Cunha, Maria das Graças</creatorcontrib><creatorcontrib>Correia, Maria Tereza dos Santos</creatorcontrib><title>Purification, characterization and antibacterial potential of a lectin isolated from Apuleia leiocarpa seeds</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>Apuleia leiocarpa is a tree found in Caatinga that has great value in the timber industry. Lectins are carbohydrate-binding proteins with several biotechnological applications. This study shows the isolation, characterization, and antibacterial activity of A. leiocarpa seed lectin (ApulSL). The lectin was chromatographically isolated from a crude extract (in 150mM NaCl) by using a chitin column. ApulSL adsorbed to the matrix and was eluted using 1.0M acetic acid. Native ApulSL was characterized as a 55.8-kDa acidic protein. SDS-PAGE showed three polypeptide bands, whereas two-dimensional electrophoresis revealed four spots. The peptides detected by MALDI TOF/TOF did not show sufficient homology (<30%) with the database proteins. Circular dichroism spectroscopy suggested a disordered conformational structure, and fluorescence spectrum showed the presence of tyrosine residues in the hydrophobic core. The hemagglutinating activity of ApulSL was present even after heating to 100°C, was Mn2+-dependent, and inhibited by N-acetylglucosamine, d(−)-arabinose, and azocasein. ApulSL demonstrated bacteriostatic and bactericide effects on gram-positive and gram-negative species, being more effective against three varieties of Xanthomonas campestris (MIC ranging from 11.2 to 22.5μg/mL and MBC of 22.5μg/mL). The results of this study reinforce the importance of biochemical prospecting of Caatinga by revealing the antibacterial potential of ApulSL.</description><subject>Animals</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Apuleia leiocarpa</subject><subject>Bacteria - drug effects</subject><subject>Chromatography, Gel</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Fabaceae - chemistry</subject><subject>Hemagglutination - drug effects</subject><subject>Hemagglutinins - chemistry</subject><subject>Humans</subject><subject>Lectin</subject><subject>Mass Spectrometry</subject><subject>Microbial Sensitivity Tests</subject><subject>Peptides - chemistry</subject><subject>Plant Lectins - chemistry</subject><subject>Plant Lectins - isolation & purification</subject><subject>Plant Lectins - pharmacology</subject><subject>Rabbits</subject><subject>Seeds - chemistry</subject><subject>Xanthomonas campestris</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P3DAQhi1UBFvKX0A-cmiCx068yQ2EaIuE1B7o2fLHWHiVxMFOKpVfj5eFXnsYzeidd2Y0DyEXwGpgIK92ddiZEEdta86grRmvGYMjsoFu21eMMfGJbBg0UHUg2Cn5nPOuqLKF7oSc8lbKTnDYkOHXmoIPVi8hTl-pfdJJ2wVTeHlTqJ5ciSWYg6oHOscFi1Cq6KmmA9olTDTkOOgFHfUpjvRmXgcM-2aIVqdZ04zo8hdy7PWQ8fw9n5Hf3-4eb39UDz-_39_ePFRWyG6puq0w2lvTOA2d7MC1wvesBdm4re_BCGm8sFYIaJ0ziI3hjecedaP7tuW9OCOXh71zis8r5kWNIVscBj1hXLMCKSXvJdvurfJgtSnmnNCrOYVRp78KmNqTVjv1QVrtSSvGVSFdBi_eb6xmRPdv7ANtMVwfDFg-_RMwqWwDThZdSIWZcjH878YrE4SU6Q</recordid><startdate>201504</startdate><enddate>201504</enddate><creator>Carvalho, Aline de Souza</creator><creator>da Silva, Márcia Vanusa</creator><creator>Gomes, Francis Soares</creator><creator>Paiva, Patrícia Maria Guedes</creator><creator>Malafaia, Carolina Barbosa</creator><creator>da Silva, Tulio Diego</creator><creator>Vaz, Antônio Fernando de Melo</creator><creator>da Silva, Alexandre Gomes</creator><creator>Arruda, Isabel Renata de Souza</creator><creator>Napoleão, Thiago Henrique</creator><creator>Carneiro-da-Cunha, Maria das Graças</creator><creator>Correia, Maria Tereza dos Santos</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-0065-2602</orcidid></search><sort><creationdate>201504</creationdate><title>Purification, characterization and antibacterial potential of a lectin isolated from Apuleia leiocarpa seeds</title><author>Carvalho, Aline de Souza ; da Silva, Márcia Vanusa ; Gomes, Francis Soares ; Paiva, Patrícia Maria Guedes ; Malafaia, Carolina Barbosa ; da Silva, Tulio Diego ; Vaz, Antônio Fernando de Melo ; da Silva, Alexandre Gomes ; Arruda, Isabel Renata de Souza ; Napoleão, Thiago Henrique ; Carneiro-da-Cunha, Maria das Graças ; Correia, Maria Tereza dos Santos</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-873bafcb4da18681d53f905164d7f91b36bf3cc3315ddbee4b24f2fea4a955293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Animals</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Apuleia leiocarpa</topic><topic>Bacteria - drug effects</topic><topic>Chromatography, Gel</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Fabaceae - chemistry</topic><topic>Hemagglutination - drug effects</topic><topic>Hemagglutinins - chemistry</topic><topic>Humans</topic><topic>Lectin</topic><topic>Mass Spectrometry</topic><topic>Microbial Sensitivity Tests</topic><topic>Peptides - chemistry</topic><topic>Plant Lectins - chemistry</topic><topic>Plant Lectins - isolation & purification</topic><topic>Plant Lectins - pharmacology</topic><topic>Rabbits</topic><topic>Seeds - chemistry</topic><topic>Xanthomonas campestris</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carvalho, Aline de Souza</creatorcontrib><creatorcontrib>da Silva, Márcia Vanusa</creatorcontrib><creatorcontrib>Gomes, Francis Soares</creatorcontrib><creatorcontrib>Paiva, Patrícia Maria Guedes</creatorcontrib><creatorcontrib>Malafaia, Carolina Barbosa</creatorcontrib><creatorcontrib>da Silva, Tulio Diego</creatorcontrib><creatorcontrib>Vaz, Antônio Fernando de Melo</creatorcontrib><creatorcontrib>da Silva, Alexandre Gomes</creatorcontrib><creatorcontrib>Arruda, Isabel Renata de Souza</creatorcontrib><creatorcontrib>Napoleão, Thiago Henrique</creatorcontrib><creatorcontrib>Carneiro-da-Cunha, Maria das Graças</creatorcontrib><creatorcontrib>Correia, Maria Tereza dos Santos</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carvalho, Aline de Souza</au><au>da Silva, Márcia Vanusa</au><au>Gomes, Francis Soares</au><au>Paiva, Patrícia Maria Guedes</au><au>Malafaia, Carolina Barbosa</au><au>da Silva, Tulio Diego</au><au>Vaz, Antônio Fernando de Melo</au><au>da Silva, Alexandre Gomes</au><au>Arruda, Isabel Renata de Souza</au><au>Napoleão, Thiago Henrique</au><au>Carneiro-da-Cunha, Maria das Graças</au><au>Correia, Maria Tereza dos Santos</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, characterization and antibacterial potential of a lectin isolated from Apuleia leiocarpa seeds</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2015-04</date><risdate>2015</risdate><volume>75</volume><spage>402</spage><epage>408</epage><pages>402-408</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>Apuleia leiocarpa is a tree found in Caatinga that has great value in the timber industry. Lectins are carbohydrate-binding proteins with several biotechnological applications. This study shows the isolation, characterization, and antibacterial activity of A. leiocarpa seed lectin (ApulSL). The lectin was chromatographically isolated from a crude extract (in 150mM NaCl) by using a chitin column. ApulSL adsorbed to the matrix and was eluted using 1.0M acetic acid. Native ApulSL was characterized as a 55.8-kDa acidic protein. SDS-PAGE showed three polypeptide bands, whereas two-dimensional electrophoresis revealed four spots. The peptides detected by MALDI TOF/TOF did not show sufficient homology (<30%) with the database proteins. Circular dichroism spectroscopy suggested a disordered conformational structure, and fluorescence spectrum showed the presence of tyrosine residues in the hydrophobic core. The hemagglutinating activity of ApulSL was present even after heating to 100°C, was Mn2+-dependent, and inhibited by N-acetylglucosamine, d(−)-arabinose, and azocasein. ApulSL demonstrated bacteriostatic and bactericide effects on gram-positive and gram-negative species, being more effective against three varieties of Xanthomonas campestris (MIC ranging from 11.2 to 22.5μg/mL and MBC of 22.5μg/mL). The results of this study reinforce the importance of biochemical prospecting of Caatinga by revealing the antibacterial potential of ApulSL.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>25668321</pmid><doi>10.1016/j.ijbiomac.2015.02.001</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-0065-2602</orcidid></addata></record> |
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| identifier | ISSN: 0141-8130 |
| ispartof | International journal of biological macromolecules, 2015-04, Vol.75, p.402-408 |
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| subjects | Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology Apuleia leiocarpa Bacteria - drug effects Chromatography, Gel Electrophoresis, Gel, Two-Dimensional Fabaceae - chemistry Hemagglutination - drug effects Hemagglutinins - chemistry Humans Lectin Mass Spectrometry Microbial Sensitivity Tests Peptides - chemistry Plant Lectins - chemistry Plant Lectins - isolation & purification Plant Lectins - pharmacology Rabbits Seeds - chemistry Xanthomonas campestris |
| title | Purification, characterization and antibacterial potential of a lectin isolated from Apuleia leiocarpa seeds |
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