Publicação
Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity
| Resumo: | Fish protein hydrolysates (FPH) obtained from industrial processing residues are sources of bioactive peptides. The enzymatic hydrolysis process is essential in obtaining specific bioactivities such as inhibition of the enzyme acetylcholinesterase (AChE). In this study the effect of different hydrolysis conditions on the properties of FPH to inhibit the enzyme acetylcholinesterase. A chemometric evaluation, based on a central composite rotatable design and principal component analysis, was applied to select hydrolysis conditions with best yield, degree of hydrolysis and acetylcholinesterase inhibition. Experimental design results for AChE inhibition were between 10.51 and 40.45% (20, 30 and 50 mg.mL-1 of FPH), and three hydrolysis conditions were selected based on PCA evaluation. The amino acids profile, FTIR and AChE inhibition kinetics were evaluated. Results showed a mixed type of inhibition behavior and, the docking molecular analyzes suggest that the inhibition AChE occurred due to the basic amino acids, mainly by arginine. |
|---|---|
| Autores principais: | Moreira, Thaysa Fernandes Moya |
| Outros Autores: | Pessoa, Luiz Gustavo Antunes; Seixas, Flávio Augusto Vicente; Ineu, Rafael P.; Gonçalves, Odinei Hess; Leimann, Fernanda Vitória; Ribeiro, Ricardo Pereira |
| Assunto: | Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase |
| Ano: | 2022 |
| País: | Portugal |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Instituto Politécnico de Bragança |
| Idioma: | inglês |
| Origem: | Biblioteca Digital do IPB |
| _version_ | 1867173050636566528 |
|---|---|
| author | Moreira, Thaysa Fernandes Moya |
| author2 | Pessoa, Luiz Gustavo Antunes Seixas, Flávio Augusto Vicente Ineu, Rafael P. Gonçalves, Odinei Hess Leimann, Fernanda Vitória Ribeiro, Ricardo Pereira |
| author2_role | author author author author author author |
| author_facet | Moreira, Thaysa Fernandes Moya Pessoa, Luiz Gustavo Antunes Seixas, Flávio Augusto Vicente Ineu, Rafael P. Gonçalves, Odinei Hess Leimann, Fernanda Vitória Ribeiro, Ricardo Pereira |
| author_role | author |
| contributor_name_str_mv | Biblioteca Digital do IPB |
| country_str | PT |
| creators_json_txt | [{\"Person.name\":\"Moreira, Thaysa Fernandes Moya\"},{\"Person.name\":\"Pessoa, Luiz Gustavo Antunes\"},{\"Person.name\":\"Seixas, Flávio Augusto Vicente\"},{\"Person.name\":\"Ineu, Rafael P.\"},{\"Person.name\":\"Gonçalves, Odinei Hess\",\"Person.identifier.orcid\":\"0000-0002-9528-8187\"},{\"Person.name\":\"Leimann, Fernanda Vitória\",\"Person.identifier.orcid\":\"0000-0001-6230-9597\"},{\"Person.name\":\"Ribeiro, Ricardo Pereira\"}] |
| datacite.contributors.contributor.contributorName.fl_str_mv | Biblioteca Digital do IPB |
| datacite.creators.creator.creatorName.fl_str_mv | Moreira, Thaysa Fernandes Moya Pessoa, Luiz Gustavo Antunes Seixas, Flávio Augusto Vicente Ineu, Rafael P. Gonçalves, Odinei Hess Leimann, Fernanda Vitória Ribeiro, Ricardo Pereira |
| datacite.date.Accepted.fl_str_mv | 2022-01-01T00:00:00Z |
| datacite.date.available.fl_str_mv | 2021-08-31T10:26:20Z |
| datacite.date.embargoed.fl_str_mv | 2021-08-31T10:26:20Z |
| datacite.rights.fl_str_mv | http://purl.org/coar/access_right/c_abf2 |
| datacite.subjects.subject.fl_str_mv | Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase |
| datacite.titles.title.fl_str_mv | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| dc.contributor.none.fl_str_mv | Biblioteca Digital do IPB |
| dc.creator.none.fl_str_mv | Moreira, Thaysa Fernandes Moya Pessoa, Luiz Gustavo Antunes Seixas, Flávio Augusto Vicente Ineu, Rafael P. Gonçalves, Odinei Hess Leimann, Fernanda Vitória Ribeiro, Ricardo Pereira |
| dc.date.Accepted.fl_str_mv | 2022-01-01T00:00:00Z |
| dc.date.available.fl_str_mv | 2021-08-31T10:26:20Z |
| dc.date.embargoed.fl_str_mv | 2021-08-31T10:26:20Z |
| dc.format.none.fl_str_mv | application/pdf |
| dc.identifier.none.fl_str_mv | http://hdl.handle.net/10198/23839 |
| dc.language.none.fl_str_mv | eng |
| dc.rights.cclincense.fl_str_mv | http://creativecommons.org/licenses/by/4.0/ |
| dc.rights.none.fl_str_mv | http://purl.org/coar/access_right/c_abf2 |
| dc.subject.none.fl_str_mv | Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase |
| dc.title.fl_str_mv | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| dc.type.none.fl_str_mv | http://purl.org/coar/resource_type/c_6501 |
| description | Fish protein hydrolysates (FPH) obtained from industrial processing residues are sources of bioactive peptides. The enzymatic hydrolysis process is essential in obtaining specific bioactivities such as inhibition of the enzyme acetylcholinesterase (AChE). In this study the effect of different hydrolysis conditions on the properties of FPH to inhibit the enzyme acetylcholinesterase. A chemometric evaluation, based on a central composite rotatable design and principal component analysis, was applied to select hydrolysis conditions with best yield, degree of hydrolysis and acetylcholinesterase inhibition. Experimental design results for AChE inhibition were between 10.51 and 40.45% (20, 30 and 50 mg.mL-1 of FPH), and three hydrolysis conditions were selected based on PCA evaluation. The amino acids profile, FTIR and AChE inhibition kinetics were evaluated. Results showed a mixed type of inhibition behavior and, the docking molecular analyzes suggest that the inhibition AChE occurred due to the basic amino acids, mainly by arginine. |
| dirty | 0 |
| eu_rights_str_mv | openAccess |
| format | article |
| fulltext.url.fl_str_mv | https://bibliotecadigital.ipb.pt/bitstreams/9b2f7d1d-36df-42cb-b48a-e697cfadbc73/download |
| id | ipb_617bca233f5fa4a6ff93add0d59bec9d |
| identifier.url.fl_str_mv | http://hdl.handle.net/10198/23839 |
| instacron_str | ipb |
| institution | Instituto Politécnico de Bragança |
| instname_str | Instituto Politécnico de Bragança |
| language | eng |
| network_acronym_str | ipb |
| network_name_str | Biblioteca Digital do IPB |
| oai_identifier_str | oai:bibliotecadigital.ipb.pt:10198/23839 |
| organization_str_mv | urn:organizationAcronym:ipb |
| person_str_mv | Moreira, Thaysa Fernandes Moya Pessoa, Luiz Gustavo Antunes Seixas, Flávio Augusto Vicente Ineu, Rafael P. Gonçalves, Odinei Hess Gonçalves, Odinei Hess http://orcid.org/0000-0002-9528-8187 0000-0002-9528-8187 Leimann, Fernanda Vitória Leimann, Fernanda Vitória https://www.ciencia-id.pt/8F10-A04D-FC0D 8F10-A04D-FC0D http://orcid.org/0000-0001-6230-9597 0000-0001-6230-9597 Ribeiro, Ricardo Pereira |
| publishDate | 2022 |
| reponame_str | Biblioteca Digital do IPB |
| repository_id_str | urn:repositoryAcronym:ipb |
| service_str_mv | urn:repositoryAcronym:ipb |
| spelling | engpt_PTFish protein hydrolysates (FPH) obtained from industrial processing residues are sources of bioactive peptides. The enzymatic hydrolysis process is essential in obtaining specific bioactivities such as inhibition of the enzyme acetylcholinesterase (AChE). In this study the effect of different hydrolysis conditions on the properties of FPH to inhibit the enzyme acetylcholinesterase. A chemometric evaluation, based on a central composite rotatable design and principal component analysis, was applied to select hydrolysis conditions with best yield, degree of hydrolysis and acetylcholinesterase inhibition. Experimental design results for AChE inhibition were between 10.51 and 40.45% (20, 30 and 50 mg.mL-1 of FPH), and three hydrolysis conditions were selected based on PCA evaluation. The amino acids profile, FTIR and AChE inhibition kinetics were evaluated. Results showed a mixed type of inhibition behavior and, the docking molecular analyzes suggest that the inhibition AChE occurred due to the basic amino acids, mainly by arginine.application/pdfpt_PTChemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activityMoreira, Thaysa Fernandes MoyaPessoa, Luiz Gustavo AntunesSeixas, Flávio Augusto VicenteIneu, Rafael P.PersonalGonçalves, Odinei HessDSpacehttp://dspace.org/items/84c8eea0-77bb-4c18-b9d8-46f865980706DSpacehttp://dspace.org/items/84c8eea0-77bb-4c18-b9d8-46f865980706GonçalvesOdinei HessORCIDhttp://orcid.org0000-0002-9528-8187Scopus Author IDhttps://www.scopus.com9335958400PersonalLeimann, Fernanda VitóriaDSpacehttp://dspace.org/items/b1102a0b-38dc-4caa-baed-ad52ccd9b230DSpacehttp://dspace.org/items/b1102a0b-38dc-4caa-baed-ad52ccd9b230LeimannFernanda VitóriaCiência IDhttps://www.ciencia-id.pt8F10-A04D-FC0DORCIDhttp://orcid.org0000-0001-6230-9597Ribeiro, Ricardo PereiraHostingInstitutionOrganizationalBiblioteca Digital do IPBe-mailmailto:dspace@ipb.ptdspace@ipb.ptISSNIsPartOf0308-8146DOIIsPartOf10.1016/j.foodchem.2021.1307282021-08-31T10:26:20Z20222022-01-01T00:00:00ZHandlehttp://hdl.handle.net/10198/23839http://purl.org/coar/access_right/c_abf2open accessFish protein hydrolysatesEnzymatic hydrolysisExperimental designAcetylcholinesterase2205813 bytesliteraturehttp://purl.org/coar/resource_type/c_6501journal article2022http://creativecommons.org/licenses/by/4.0/http://purl.org/coar/access_right/c_abf2application/pdffulltexthttps://bibliotecadigital.ipb.pt/bitstreams/9b2f7d1d-36df-42cb-b48a-e697cfadbc73/downloadFood Chemistry367130728 |
| spellingShingle | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity Moreira, Thaysa Fernandes Moya Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase |
| status | SINGLETON |
| subject.fl_str_mv | Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase |
| title | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| title_full | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| title_fullStr | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| title_full_unstemmed | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| title_short | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| title_sort | Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity |
| topic | Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase |
| topic_facet | Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase |
| url | http://hdl.handle.net/10198/23839 |
| visible | 1 |