Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes

Detalhes bibliográficos
Autor(a) principal: Santos, Sarita D’Avila dos
Data de Publicação: 2011
Outros Autores: Martins, Vilásia Guimarães, Salas-Mellado, Myriam de las Mercedes, Hernandez, Carlos Prentice
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da FURG (RI FURG)
Texto Completo: http://repositorio.furg.br/handle/1/1729
Resumo: Enzymatic hydrolysis of proteins from low commercial value fish could be produced for uses like functional ingredients in a wide and always increasing zone of application in different food products. The objective of this work was to evaluate the functional properties and the amino acid profile of enzymatic hydrolysates from Bluewing searobin (Prionotus punctatus), using two microbial enzymes, Alcalase and Flavourzyme. The enzymatic hydrolysate obtained through the addition of the enzyme Alcalase reached the maximum solubility (42%) at pH 9, water holding capacity (WHC) of 2.4 gwater gprotein−1, 4.5 goil gprotein−1 of oil holding capacity (OHC) and an emulsifying activity index (EAI) of 54 m2 gsolids−1 at pH 3. On the other hand, the hydrolysate obtained from Flavourzyme attained 38% of solubility at pH 9, 3.7 gwater gprotein−1 and 5.5 goil gprotein−1 for the holding capacities, and an EAI of 71 m2 gsolids−1 at pH 11. The hydrolysate with Flavourzyme produced best results for WHC, OHC, and EAI because it had solubility lower than the hydrolysate of Alcalase. The hydrolysate produced by Alcalase had a higher amino acid content compared with Flavourzyme’s hydrolysate. However, both showed a good essential amino acid amounts. In general, these results indicate the potential utilization of the hydrolysate from Bluewing searobin in food formulations for the direct human consumption.
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spelling Santos, Sarita D’Avila dosMartins, Vilásia GuimarãesSalas-Mellado, Myriam de las MercedesHernandez, Carlos Prentice2012-01-07T23:56:11Z2012-01-07T23:56:11Z2011SANTOS, Sarita D’Avila dos et al. Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes. Food Bioprocess Technol. v. 4, n. 8, p. 1399–1406, 2011. Disponível em: <http://www.springerlink.com/content/hj58216j1448h885/fulltext.pdf> Acesso em: 19 dez. 2011.1935-5130http://repositorio.furg.br/handle/1/172910.1007/s11947-009-0301-0Enzymatic hydrolysis of proteins from low commercial value fish could be produced for uses like functional ingredients in a wide and always increasing zone of application in different food products. The objective of this work was to evaluate the functional properties and the amino acid profile of enzymatic hydrolysates from Bluewing searobin (Prionotus punctatus), using two microbial enzymes, Alcalase and Flavourzyme. The enzymatic hydrolysate obtained through the addition of the enzyme Alcalase reached the maximum solubility (42%) at pH 9, water holding capacity (WHC) of 2.4 gwater gprotein−1, 4.5 goil gprotein−1 of oil holding capacity (OHC) and an emulsifying activity index (EAI) of 54 m2 gsolids−1 at pH 3. On the other hand, the hydrolysate obtained from Flavourzyme attained 38% of solubility at pH 9, 3.7 gwater gprotein−1 and 5.5 goil gprotein−1 for the holding capacities, and an EAI of 71 m2 gsolids−1 at pH 11. The hydrolysate with Flavourzyme produced best results for WHC, OHC, and EAI because it had solubility lower than the hydrolysate of Alcalase. The hydrolysate produced by Alcalase had a higher amino acid content compared with Flavourzyme’s hydrolysate. However, both showed a good essential amino acid amounts. In general, these results indicate the potential utilization of the hydrolysate from Bluewing searobin in food formulations for the direct human consumption.engFishEnzymatic hydrolysatesAlcalaseFlavourzymeFunctional propertiesEvaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da FURG (RI FURG)instname:Universidade Federal do Rio Grande (FURG)instacron:FURGORIGINALEvaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes.pdfEvaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes.pdfapplication/pdf201541https://repositorio.furg.br/bitstream/1/1729/1/Evaluation%20of%20functional%20properties%20in%20protein%20hydrolysates%20from%20bluewing%20searobin%20%28prionotus%20punctatus%29%20obtained%20with%20different%20microbial%20enzymes.pdf270c06f27d87203916882d75a9992c8eMD51open accessLICENSElicense.txtlicense.txttext/plain; charset=utf-81724https://repositorio.furg.br/bitstream/1/1729/2/license.txt5b92b9704b4f13242d70e45ddef35a68MD52open access1/17292019-12-03 22:02:48.241open accessoai:repositorio.furg.br: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Repositório InstitucionalPUBhttps://repositorio.furg.br/oai/request || http://200.19.254.174/oai/requestopendoar:2019-12-04T01:02:48Repositório Institucional da FURG (RI FURG) - Universidade Federal do Rio Grande (FURG)false
dc.title.pt_BR.fl_str_mv Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
title Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
spellingShingle Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
Santos, Sarita D’Avila dos
Fish
Enzymatic hydrolysates
Alcalase
Flavourzyme
Functional properties
title_short Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
title_full Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
title_fullStr Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
title_full_unstemmed Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
title_sort Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes
author Santos, Sarita D’Avila dos
author_facet Santos, Sarita D’Avila dos
Martins, Vilásia Guimarães
Salas-Mellado, Myriam de las Mercedes
Hernandez, Carlos Prentice
author_role author
author2 Martins, Vilásia Guimarães
Salas-Mellado, Myriam de las Mercedes
Hernandez, Carlos Prentice
author2_role author
author
author
dc.contributor.author.fl_str_mv Santos, Sarita D’Avila dos
Martins, Vilásia Guimarães
Salas-Mellado, Myriam de las Mercedes
Hernandez, Carlos Prentice
dc.subject.por.fl_str_mv Fish
Enzymatic hydrolysates
Alcalase
Flavourzyme
Functional properties
topic Fish
Enzymatic hydrolysates
Alcalase
Flavourzyme
Functional properties
description Enzymatic hydrolysis of proteins from low commercial value fish could be produced for uses like functional ingredients in a wide and always increasing zone of application in different food products. The objective of this work was to evaluate the functional properties and the amino acid profile of enzymatic hydrolysates from Bluewing searobin (Prionotus punctatus), using two microbial enzymes, Alcalase and Flavourzyme. The enzymatic hydrolysate obtained through the addition of the enzyme Alcalase reached the maximum solubility (42%) at pH 9, water holding capacity (WHC) of 2.4 gwater gprotein−1, 4.5 goil gprotein−1 of oil holding capacity (OHC) and an emulsifying activity index (EAI) of 54 m2 gsolids−1 at pH 3. On the other hand, the hydrolysate obtained from Flavourzyme attained 38% of solubility at pH 9, 3.7 gwater gprotein−1 and 5.5 goil gprotein−1 for the holding capacities, and an EAI of 71 m2 gsolids−1 at pH 11. The hydrolysate with Flavourzyme produced best results for WHC, OHC, and EAI because it had solubility lower than the hydrolysate of Alcalase. The hydrolysate produced by Alcalase had a higher amino acid content compared with Flavourzyme’s hydrolysate. However, both showed a good essential amino acid amounts. In general, these results indicate the potential utilization of the hydrolysate from Bluewing searobin in food formulations for the direct human consumption.
publishDate 2011
dc.date.issued.fl_str_mv 2011
dc.date.accessioned.fl_str_mv 2012-01-07T23:56:11Z
dc.date.available.fl_str_mv 2012-01-07T23:56:11Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.citation.fl_str_mv SANTOS, Sarita D’Avila dos et al. Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes. Food Bioprocess Technol. v. 4, n. 8, p. 1399–1406, 2011. Disponível em: <http://www.springerlink.com/content/hj58216j1448h885/fulltext.pdf> Acesso em: 19 dez. 2011.
dc.identifier.uri.fl_str_mv http://repositorio.furg.br/handle/1/1729
dc.identifier.issn.none.fl_str_mv 1935-5130
dc.identifier.doi.pt_BR.fl_str_mv 10.1007/s11947-009-0301-0
identifier_str_mv SANTOS, Sarita D’Avila dos et al. Evaluation of functional properties in protein hydrolysates from bluewing searobin (prionotus punctatus) obtained with different microbial enzymes. Food Bioprocess Technol. v. 4, n. 8, p. 1399–1406, 2011. Disponível em: <http://www.springerlink.com/content/hj58216j1448h885/fulltext.pdf> Acesso em: 19 dez. 2011.
1935-5130
10.1007/s11947-009-0301-0
url http://repositorio.furg.br/handle/1/1729
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institution FURG
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