Immobilization of Horseradish Peroxidase on Ca Alginate-Starch Hybrid Support: Biocatalytic Properties and Application in Biodegradation of Phenol Red Dye
In this study, horseradish peroxidase was extracted, purified, and immobilized on a calcium alginate-starch hybrid support by covalent bonding and entrapment. The immobilized HRP was used for the biodegradation of phenol red dye. A 3.74-fold purification was observed after precipitation with ammoniu...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2024-08, Vol.196 (8), p.4759-4792 |
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| creator | Weber, Ani Caroline da Silva, Bruno Eduardo Cordeiro, Sabrina Grando Henn, Guilherme Schwingel Costa, Bruna dos Santos, Jéssica Samara Herek Corbellini, Valeriano Antonio Ethur, Eduardo Miranda Hoehne, Lucélia |
| description | In this study, horseradish peroxidase was extracted, purified, and immobilized on a calcium alginate-starch hybrid support by covalent bonding and entrapment. The immobilized HRP was used for the biodegradation of phenol red dye. A 3.74-fold purification was observed after precipitation with ammonium sulfate and dialysis. An immobilization yield of 88.33%, efficiency of 56.89%, and activity recovery of 50.26% were found. The optimum pH and temperature values for immobilized and free HRP were 5.0 and 50 °C and 6.5 and 60 °C, respectively. The immobilized HRP showed better thermal stability than its free form, resulting in a considerable increase in half-life time (t
1/2
) and deactivation energy (E
d
). The immobilized HRP maintained 93.71% of its initial activity after 45 days of storage at 4 °C. Regarding the biodegradation of phenol red, immobilized HRP resulted in 63.57% degradation after 90 min. After 10 cycles of reuse, the immobilized HRP was able to maintain 43.06% of its initial biodegradative capacity and 42.36% of its enzymatic activity. At the end of 15 application cycles, a biodegradation rate of 8.34% was observed. In conclusion, the results demonstrate that the immobilized HRP is a promising option for use as an industrial biocatalyst in various biotechnological applications. |
| doi_str_mv | 10.1007/s12010-023-04772-8 |
| format | Article |
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1/2
) and deactivation energy (E
d
). The immobilized HRP maintained 93.71% of its initial activity after 45 days of storage at 4 °C. Regarding the biodegradation of phenol red, immobilized HRP resulted in 63.57% degradation after 90 min. After 10 cycles of reuse, the immobilized HRP was able to maintain 43.06% of its initial biodegradative capacity and 42.36% of its enzymatic activity. At the end of 15 application cycles, a biodegradation rate of 8.34% was observed. In conclusion, the results demonstrate that the immobilized HRP is a promising option for use as an industrial biocatalyst in various biotechnological applications.</description><identifier>ISSN: 0273-2289</identifier><identifier>ISSN: 1559-0291</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-023-04772-8</identifier><identifier>PMID: 37950796</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Alginates - chemistry ; Alginic acid ; Ammonium ; Ammonium sulfate ; Biocatalysis ; biocatalysts ; Biochemistry ; Biodegradation ; Biodegradation, Environmental ; Biotechnology ; calcium ; Calcium alginate ; Chemistry ; Chemistry and Materials Science ; Coloring Agents - chemistry ; Coloring Agents - metabolism ; Dialysis ; Dyes ; energy ; Entrapment ; Enzymatic activity ; enzyme activity ; Enzyme Stability ; Enzymes, Immobilized - chemistry ; Enzymes, Immobilized - metabolism ; Free form ; Glucuronic Acid - chemistry ; half life ; Hexuronic Acids - chemistry ; Horseradish peroxidase ; Horseradish Peroxidase - chemistry ; Horseradish Peroxidase - metabolism ; Hydrogen-Ion Concentration ; Immobilization ; Original Article ; Peroxidase ; Phenols ; phenolsulfonphthalein ; Phenolsulfonphthalein - chemistry ; Starch ; Starch - chemistry ; Starch - metabolism ; Temperature ; Thermal stability</subject><ispartof>Applied biochemistry and biotechnology, 2024-08, Vol.196 (8), p.4759-4792</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-735dd5e8136f0a04c673d7aa2b9272d9d96fb98515a491fe97093ca955a4d9503</citedby><cites>FETCH-LOGICAL-c408t-735dd5e8136f0a04c673d7aa2b9272d9d96fb98515a491fe97093ca955a4d9503</cites><orcidid>0000-0002-3221-7007</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-023-04772-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-023-04772-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37950796$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Weber, Ani Caroline</creatorcontrib><creatorcontrib>da Silva, Bruno Eduardo</creatorcontrib><creatorcontrib>Cordeiro, Sabrina Grando</creatorcontrib><creatorcontrib>Henn, Guilherme Schwingel</creatorcontrib><creatorcontrib>Costa, Bruna</creatorcontrib><creatorcontrib>dos Santos, Jéssica Samara Herek</creatorcontrib><creatorcontrib>Corbellini, Valeriano Antonio</creatorcontrib><creatorcontrib>Ethur, Eduardo Miranda</creatorcontrib><creatorcontrib>Hoehne, Lucélia</creatorcontrib><title>Immobilization of Horseradish Peroxidase on Ca Alginate-Starch Hybrid Support: Biocatalytic Properties and Application in Biodegradation of Phenol Red Dye</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>In this study, horseradish peroxidase was extracted, purified, and immobilized on a calcium alginate-starch hybrid support by covalent bonding and entrapment. The immobilized HRP was used for the biodegradation of phenol red dye. A 3.74-fold purification was observed after precipitation with ammonium sulfate and dialysis. An immobilization yield of 88.33%, efficiency of 56.89%, and activity recovery of 50.26% were found. The optimum pH and temperature values for immobilized and free HRP were 5.0 and 50 °C and 6.5 and 60 °C, respectively. The immobilized HRP showed better thermal stability than its free form, resulting in a considerable increase in half-life time (t
1/2
) and deactivation energy (E
d
). The immobilized HRP maintained 93.71% of its initial activity after 45 days of storage at 4 °C. Regarding the biodegradation of phenol red, immobilized HRP resulted in 63.57% degradation after 90 min. After 10 cycles of reuse, the immobilized HRP was able to maintain 43.06% of its initial biodegradative capacity and 42.36% of its enzymatic activity. At the end of 15 application cycles, a biodegradation rate of 8.34% was observed. In conclusion, the results demonstrate that the immobilized HRP is a promising option for use as an industrial biocatalyst in various biotechnological applications.</description><subject>Alginates - chemistry</subject><subject>Alginic acid</subject><subject>Ammonium</subject><subject>Ammonium sulfate</subject><subject>Biocatalysis</subject><subject>biocatalysts</subject><subject>Biochemistry</subject><subject>Biodegradation</subject><subject>Biodegradation, Environmental</subject><subject>Biotechnology</subject><subject>calcium</subject><subject>Calcium alginate</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Coloring Agents - chemistry</subject><subject>Coloring Agents - metabolism</subject><subject>Dialysis</subject><subject>Dyes</subject><subject>energy</subject><subject>Entrapment</subject><subject>Enzymatic activity</subject><subject>enzyme activity</subject><subject>Enzyme Stability</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Free form</subject><subject>Glucuronic Acid - chemistry</subject><subject>half life</subject><subject>Hexuronic Acids - chemistry</subject><subject>Horseradish peroxidase</subject><subject>Horseradish Peroxidase - chemistry</subject><subject>Horseradish Peroxidase - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immobilization</subject><subject>Original Article</subject><subject>Peroxidase</subject><subject>Phenols</subject><subject>phenolsulfonphthalein</subject><subject>Phenolsulfonphthalein - chemistry</subject><subject>Starch</subject><subject>Starch - chemistry</subject><subject>Starch - metabolism</subject><subject>Temperature</subject><subject>Thermal stability</subject><issn>0273-2289</issn><issn>1559-0291</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EokPhBVggS2zYBPwTxza7YfiZSpUYUVhbTnwz4yqJg51ITB-lT4uHlCKxgJVl38_n3HsPQs8peU0JkW8SZYSSgjBekFJKVqgHaEWF0PlJ04doRZjkBWNKn6EnKV0TQpkS8jE641ILInW1QrcXfR9q3_kbO_kw4NDibYgJonU-HfAOYvjhnU2Ac3Fj8brb-8FOUFxNNjYHvD3W0Tt8NY9jiNNb_M6Hxk62O06-wbsYRoiTh4Tt4PB6HDvfLD5-OKEO9tno3nl3gCF0-As4_P4IT9Gj1nYJnt2d5-jbxw9fN9vi8vOni836smhKoqZCcuGcAEV51RJLyqaS3ElrWa2ZZE47XbW1VoIKW2ragpZE88Zqke8ur4Gfo1eL7hjD9xnSZHqfGug6O0CYk-FUcKm4rNR_UaaUZiUVVZnRl3-h12GOQx4kC5Kyyr1XVabYQjUxpBShNWP0vY1HQ4k5hWyWkE0O2fwK2Zy6eHEnPdc9uPsvv1PNAF-AlEvDHuIf73_I_gSGF7Kk</recordid><startdate>20240801</startdate><enddate>20240801</enddate><creator>Weber, Ani Caroline</creator><creator>da Silva, Bruno Eduardo</creator><creator>Cordeiro, Sabrina Grando</creator><creator>Henn, Guilherme Schwingel</creator><creator>Costa, Bruna</creator><creator>dos Santos, Jéssica Samara Herek</creator><creator>Corbellini, Valeriano Antonio</creator><creator>Ethur, Eduardo Miranda</creator><creator>Hoehne, Lucélia</creator><general>Springer US</general><general>Springer Nature 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>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0002-3221-7007</orcidid></search><sort><creationdate>20240801</creationdate><title>Immobilization of Horseradish Peroxidase on Ca Alginate-Starch Hybrid Support: Biocatalytic Properties and Application in Biodegradation of Phenol Red Dye</title><author>Weber, Ani Caroline ; da Silva, Bruno Eduardo ; Cordeiro, Sabrina Grando ; Henn, Guilherme Schwingel ; Costa, Bruna ; dos Santos, Jéssica Samara Herek ; Corbellini, Valeriano Antonio ; Ethur, Eduardo Miranda ; Hoehne, Lucélia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-735dd5e8136f0a04c673d7aa2b9272d9d96fb98515a491fe97093ca955a4d9503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Alginates - chemistry</topic><topic>Alginic acid</topic><topic>Ammonium</topic><topic>Ammonium sulfate</topic><topic>Biocatalysis</topic><topic>biocatalysts</topic><topic>Biochemistry</topic><topic>Biodegradation</topic><topic>Biodegradation, Environmental</topic><topic>Biotechnology</topic><topic>calcium</topic><topic>Calcium alginate</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Coloring Agents - chemistry</topic><topic>Coloring Agents - metabolism</topic><topic>Dialysis</topic><topic>Dyes</topic><topic>energy</topic><topic>Entrapment</topic><topic>Enzymatic activity</topic><topic>enzyme activity</topic><topic>Enzyme Stability</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Enzymes, Immobilized - metabolism</topic><topic>Free form</topic><topic>Glucuronic Acid - chemistry</topic><topic>half life</topic><topic>Hexuronic Acids - chemistry</topic><topic>Horseradish peroxidase</topic><topic>Horseradish Peroxidase - chemistry</topic><topic>Horseradish Peroxidase - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immobilization</topic><topic>Original Article</topic><topic>Peroxidase</topic><topic>Phenols</topic><topic>phenolsulfonphthalein</topic><topic>Phenolsulfonphthalein - chemistry</topic><topic>Starch</topic><topic>Starch - chemistry</topic><topic>Starch - metabolism</topic><topic>Temperature</topic><topic>Thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Weber, Ani Caroline</creatorcontrib><creatorcontrib>da Silva, Bruno Eduardo</creatorcontrib><creatorcontrib>Cordeiro, Sabrina Grando</creatorcontrib><creatorcontrib>Henn, Guilherme Schwingel</creatorcontrib><creatorcontrib>Costa, Bruna</creatorcontrib><creatorcontrib>dos Santos, Jéssica Samara Herek</creatorcontrib><creatorcontrib>Corbellini, Valeriano Antonio</creatorcontrib><creatorcontrib>Ethur, Eduardo Miranda</creatorcontrib><creatorcontrib>Hoehne, Lucélia</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Weber, Ani Caroline</au><au>da Silva, Bruno Eduardo</au><au>Cordeiro, Sabrina Grando</au><au>Henn, Guilherme Schwingel</au><au>Costa, Bruna</au><au>dos Santos, Jéssica Samara Herek</au><au>Corbellini, Valeriano Antonio</au><au>Ethur, Eduardo Miranda</au><au>Hoehne, Lucélia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilization of Horseradish Peroxidase on Ca Alginate-Starch Hybrid Support: Biocatalytic Properties and Application in Biodegradation of Phenol Red Dye</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2024-08-01</date><risdate>2024</risdate><volume>196</volume><issue>8</issue><spage>4759</spage><epage>4792</epage><pages>4759-4792</pages><issn>0273-2289</issn><issn>1559-0291</issn><eissn>1559-0291</eissn><abstract>In this study, horseradish peroxidase was extracted, purified, and immobilized on a calcium alginate-starch hybrid support by covalent bonding and entrapment. The immobilized HRP was used for the biodegradation of phenol red dye. A 3.74-fold purification was observed after precipitation with ammonium sulfate and dialysis. An immobilization yield of 88.33%, efficiency of 56.89%, and activity recovery of 50.26% were found. The optimum pH and temperature values for immobilized and free HRP were 5.0 and 50 °C and 6.5 and 60 °C, respectively. The immobilized HRP showed better thermal stability than its free form, resulting in a considerable increase in half-life time (t
1/2
) and deactivation energy (E
d
). The immobilized HRP maintained 93.71% of its initial activity after 45 days of storage at 4 °C. Regarding the biodegradation of phenol red, immobilized HRP resulted in 63.57% degradation after 90 min. After 10 cycles of reuse, the immobilized HRP was able to maintain 43.06% of its initial biodegradative capacity and 42.36% of its enzymatic activity. At the end of 15 application cycles, a biodegradation rate of 8.34% was observed. In conclusion, the results demonstrate that the immobilized HRP is a promising option for use as an industrial biocatalyst in various biotechnological applications.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>37950796</pmid><doi>10.1007/s12010-023-04772-8</doi><tpages>34</tpages><orcidid>https://orcid.org/0000-0002-3221-7007</orcidid></addata></record> |
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| subjects | Alginates - chemistry Alginic acid Ammonium Ammonium sulfate Biocatalysis biocatalysts Biochemistry Biodegradation Biodegradation, Environmental Biotechnology calcium Calcium alginate Chemistry Chemistry and Materials Science Coloring Agents - chemistry Coloring Agents - metabolism Dialysis Dyes energy Entrapment Enzymatic activity enzyme activity Enzyme Stability Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Free form Glucuronic Acid - chemistry half life Hexuronic Acids - chemistry Horseradish peroxidase Horseradish Peroxidase - chemistry Horseradish Peroxidase - metabolism Hydrogen-Ion Concentration Immobilization Original Article Peroxidase Phenols phenolsulfonphthalein Phenolsulfonphthalein - chemistry Starch Starch - chemistry Starch - metabolism Temperature Thermal stability |
| title | Immobilization of Horseradish Peroxidase on Ca Alginate-Starch Hybrid Support: Biocatalytic Properties and Application in Biodegradation of Phenol Red Dye |
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