Efficiency Assessment between Entrapment and Covalent Bond Immobilization of Mutant β-Xylosidase onto Chitosan Support
The Y509E mutant of β-xylosidase from (XynB2 ) (which also bears xylanase activity) has been immobilized in chitosan spheres through either entrapment or covalent bond formation methods. The maximum immobilization yield by entrapment was achieved by chitosan beads developed using a 2% chitosan solut...
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| Veröffentlicht in: | Polymers 2023-07, Vol.15 (15), p.3170 |
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| creator | Romero, Gabriela Contreras, Lellys M Aguirre Céspedes, Carolina Wilkesman, Jeff Clemente-Jiménez, Josefa María Rodríguez-Vico, Felipe Las Heras-Vázquez, Francisco Javier |
| description | The Y509E mutant of β-xylosidase from
(XynB2
) (which also bears xylanase activity) has been immobilized in chitosan spheres through either entrapment or covalent bond formation methods. The maximum immobilization yield by entrapment was achieved by chitosan beads developed using a 2% chitosan solution after 1 h of maturation time in CFG buffer with ethanol. On the other hand, the highest value in covalent bond immobilization was observed when employing chitosan beads that were prepared from a 2% chitosan solution after 4 h of activation in 1% glutaraldehyde solution at pH 8. The activity expressed after immobilization by covalent bonding was 23% higher compared to the activity expressed following entrapment immobilization, with values of 122.3 and 99.4 IU.g
, respectively. Kinetic data revealed that catalytic turnover values were decreased as compared to a free counterpart. Both biocatalysts showed increased thermal and pH stability, along with an improved storage capacity, as they retained 88% and 40% of their activity after being stored at 4 °C for two months. Moreover, XynB2
immobilized by covalent binding also exhibited outstanding reusability, retaining 92% of activity after 10 cycles of reuse. In conclusion, our results suggest that the covalent bond method appears to be the best choice for XynB2
immobilization. |
| doi_str_mv | 10.3390/polym15153170 |
| format | Article |
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(XynB2
) (which also bears xylanase activity) has been immobilized in chitosan spheres through either entrapment or covalent bond formation methods. The maximum immobilization yield by entrapment was achieved by chitosan beads developed using a 2% chitosan solution after 1 h of maturation time in CFG buffer with ethanol. On the other hand, the highest value in covalent bond immobilization was observed when employing chitosan beads that were prepared from a 2% chitosan solution after 4 h of activation in 1% glutaraldehyde solution at pH 8. The activity expressed after immobilization by covalent bonding was 23% higher compared to the activity expressed following entrapment immobilization, with values of 122.3 and 99.4 IU.g
, respectively. Kinetic data revealed that catalytic turnover values were decreased as compared to a free counterpart. Both biocatalysts showed increased thermal and pH stability, along with an improved storage capacity, as they retained 88% and 40% of their activity after being stored at 4 °C for two months. Moreover, XynB2
immobilized by covalent binding also exhibited outstanding reusability, retaining 92% of activity after 10 cycles of reuse. In conclusion, our results suggest that the covalent bond method appears to be the best choice for XynB2
immobilization.</description><identifier>ISSN: 2073-4360</identifier><identifier>EISSN: 2073-4360</identifier><identifier>DOI: 10.3390/polym15153170</identifier><identifier>PMID: 37571063</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acids ; Beads ; Biocatalysts ; Chemical bonds ; Chitosan ; Covalence ; Covalent bonds ; Entrapment ; Enzymes ; Ethanol ; Immobilization ; Mutagenesis ; Proteins ; Storage capacity ; Xylanase</subject><ispartof>Polymers, 2023-07, Vol.15 (15), p.3170</ispartof><rights>COPYRIGHT 2023 MDPI AG</rights><rights>2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2023 by the authors. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-e7f2f3a843eca923dba9d62b99cf14692baf3afece10ca83da23627476f6c6943</citedby><cites>FETCH-LOGICAL-c483t-e7f2f3a843eca923dba9d62b99cf14692baf3afece10ca83da23627476f6c6943</cites><orcidid>0000-0001-7260-1911 ; 0000-0002-5374-9088 ; 0000-0002-9424-9602 ; 0000-0003-4254-4551</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10421103/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10421103/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37571063$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Romero, Gabriela</creatorcontrib><creatorcontrib>Contreras, Lellys M</creatorcontrib><creatorcontrib>Aguirre Céspedes, Carolina</creatorcontrib><creatorcontrib>Wilkesman, Jeff</creatorcontrib><creatorcontrib>Clemente-Jiménez, Josefa María</creatorcontrib><creatorcontrib>Rodríguez-Vico, Felipe</creatorcontrib><creatorcontrib>Las Heras-Vázquez, Francisco Javier</creatorcontrib><title>Efficiency Assessment between Entrapment and Covalent Bond Immobilization of Mutant β-Xylosidase onto Chitosan Support</title><title>Polymers</title><addtitle>Polymers (Basel)</addtitle><description>The Y509E mutant of β-xylosidase from
(XynB2
) (which also bears xylanase activity) has been immobilized in chitosan spheres through either entrapment or covalent bond formation methods. The maximum immobilization yield by entrapment was achieved by chitosan beads developed using a 2% chitosan solution after 1 h of maturation time in CFG buffer with ethanol. On the other hand, the highest value in covalent bond immobilization was observed when employing chitosan beads that were prepared from a 2% chitosan solution after 4 h of activation in 1% glutaraldehyde solution at pH 8. The activity expressed after immobilization by covalent bonding was 23% higher compared to the activity expressed following entrapment immobilization, with values of 122.3 and 99.4 IU.g
, respectively. Kinetic data revealed that catalytic turnover values were decreased as compared to a free counterpart. Both biocatalysts showed increased thermal and pH stability, along with an improved storage capacity, as they retained 88% and 40% of their activity after being stored at 4 °C for two months. Moreover, XynB2
immobilized by covalent binding also exhibited outstanding reusability, retaining 92% of activity after 10 cycles of reuse. In conclusion, our results suggest that the covalent bond method appears to be the best choice for XynB2
immobilization.</description><subject>Amino acids</subject><subject>Beads</subject><subject>Biocatalysts</subject><subject>Chemical bonds</subject><subject>Chitosan</subject><subject>Covalence</subject><subject>Covalent bonds</subject><subject>Entrapment</subject><subject>Enzymes</subject><subject>Ethanol</subject><subject>Immobilization</subject><subject>Mutagenesis</subject><subject>Proteins</subject><subject>Storage capacity</subject><subject>Xylanase</subject><issn>2073-4360</issn><issn>2073-4360</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNptks1u1DAQxyMEolXpkSuyxIVLij8SOzmhZbVApSIOgMTNcpxx6yrxhNhptTwWD8Iz4aWl2kXYB8_Hb_7WjKYonjN6JkRLX084bEdWs1owRR8Vx5wqUVZC0sd79lFxGuM1zaeqpWTqaXEkVK0YleK4uN04562HYLdkFSPEOEJIpIN0CxDIJqTZTH9CJvRkjTdm2DlvMXvn44idH_wPkzwGgo58XJLJ2V8_y2_bAaPvTQSCISFZX_mE0QTyeZkmnNOz4okzQ4TT-_ek-Ppu82X9obz49P58vboobdWIVIJy3AnTVAKsabnoO9P2kndtax2rZMs7k9MOLDBqTSN6w4XkqlLSSSvbSpwUb-50p6Ubobewa2jQ0-xHM281Gq8PM8Ff6Uu80YxWnDEqssKre4UZvy8Qkx59tDAMJgAuUfOmpoI2VNKMvvwHvcZlDrm_TFUtbbiq96jLPEvtg8P8sd2J6pWSVDIpuMrU2X-ofHsYvcUAzuf4QUF5V2BnjHEG99Ako3q3LfpgWzL_Yn8yD_Tf3RC_AfepvW4</recordid><startdate>20230726</startdate><enddate>20230726</enddate><creator>Romero, Gabriela</creator><creator>Contreras, Lellys M</creator><creator>Aguirre Céspedes, Carolina</creator><creator>Wilkesman, Jeff</creator><creator>Clemente-Jiménez, Josefa María</creator><creator>Rodríguez-Vico, Felipe</creator><creator>Las Heras-Vázquez, Francisco Javier</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-7260-1911</orcidid><orcidid>https://orcid.org/0000-0002-5374-9088</orcidid><orcidid>https://orcid.org/0000-0002-9424-9602</orcidid><orcidid>https://orcid.org/0000-0003-4254-4551</orcidid></search><sort><creationdate>20230726</creationdate><title>Efficiency Assessment between Entrapment and Covalent Bond Immobilization of Mutant β-Xylosidase onto Chitosan Support</title><author>Romero, Gabriela ; Contreras, Lellys M ; Aguirre Céspedes, Carolina ; Wilkesman, Jeff ; Clemente-Jiménez, Josefa María ; Rodríguez-Vico, Felipe ; Las Heras-Vázquez, Francisco Javier</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-e7f2f3a843eca923dba9d62b99cf14692baf3afece10ca83da23627476f6c6943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Amino acids</topic><topic>Beads</topic><topic>Biocatalysts</topic><topic>Chemical bonds</topic><topic>Chitosan</topic><topic>Covalence</topic><topic>Covalent bonds</topic><topic>Entrapment</topic><topic>Enzymes</topic><topic>Ethanol</topic><topic>Immobilization</topic><topic>Mutagenesis</topic><topic>Proteins</topic><topic>Storage capacity</topic><topic>Xylanase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Romero, Gabriela</creatorcontrib><creatorcontrib>Contreras, Lellys M</creatorcontrib><creatorcontrib>Aguirre Céspedes, Carolina</creatorcontrib><creatorcontrib>Wilkesman, Jeff</creatorcontrib><creatorcontrib>Clemente-Jiménez, Josefa María</creatorcontrib><creatorcontrib>Rodríguez-Vico, Felipe</creatorcontrib><creatorcontrib>Las Heras-Vázquez, Francisco Javier</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>Materials Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Polymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Romero, Gabriela</au><au>Contreras, Lellys M</au><au>Aguirre Céspedes, Carolina</au><au>Wilkesman, Jeff</au><au>Clemente-Jiménez, Josefa María</au><au>Rodríguez-Vico, Felipe</au><au>Las Heras-Vázquez, Francisco Javier</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Efficiency Assessment between Entrapment and Covalent Bond Immobilization of Mutant β-Xylosidase onto Chitosan Support</atitle><jtitle>Polymers</jtitle><addtitle>Polymers (Basel)</addtitle><date>2023-07-26</date><risdate>2023</risdate><volume>15</volume><issue>15</issue><spage>3170</spage><pages>3170-</pages><issn>2073-4360</issn><eissn>2073-4360</eissn><abstract>The Y509E mutant of β-xylosidase from
(XynB2
) (which also bears xylanase activity) has been immobilized in chitosan spheres through either entrapment or covalent bond formation methods. The maximum immobilization yield by entrapment was achieved by chitosan beads developed using a 2% chitosan solution after 1 h of maturation time in CFG buffer with ethanol. On the other hand, the highest value in covalent bond immobilization was observed when employing chitosan beads that were prepared from a 2% chitosan solution after 4 h of activation in 1% glutaraldehyde solution at pH 8. The activity expressed after immobilization by covalent bonding was 23% higher compared to the activity expressed following entrapment immobilization, with values of 122.3 and 99.4 IU.g
, respectively. Kinetic data revealed that catalytic turnover values were decreased as compared to a free counterpart. Both biocatalysts showed increased thermal and pH stability, along with an improved storage capacity, as they retained 88% and 40% of their activity after being stored at 4 °C for two months. Moreover, XynB2
immobilized by covalent binding also exhibited outstanding reusability, retaining 92% of activity after 10 cycles of reuse. In conclusion, our results suggest that the covalent bond method appears to be the best choice for XynB2
immobilization.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>37571063</pmid><doi>10.3390/polym15153170</doi><orcidid>https://orcid.org/0000-0001-7260-1911</orcidid><orcidid>https://orcid.org/0000-0002-5374-9088</orcidid><orcidid>https://orcid.org/0000-0002-9424-9602</orcidid><orcidid>https://orcid.org/0000-0003-4254-4551</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MDPI - Multidisciplinary Digital Publishing Institute; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; PubMed Central Open Access |
| subjects | Amino acids Beads Biocatalysts Chemical bonds Chitosan Covalence Covalent bonds Entrapment Enzymes Ethanol Immobilization Mutagenesis Proteins Storage capacity Xylanase |
| title | Efficiency Assessment between Entrapment and Covalent Bond Immobilization of Mutant β-Xylosidase onto Chitosan Support |
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