PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Revista Brasileira de Tecnologia Agroindustrial |
Texto Completo: | https://periodicos.utfpr.edu.br/rbta/article/view/2755 |
Resumo: | The interest in collagen use in the food industry to replace synthetic agents is growing every day. Among the derivatives, has the hydrolysate, which dissolves easily in water and brine, and can be incorporated into foods or drinks. The objective of this study was to determine the degree of hydrolysis (DH) of crude collagen fiber, powdered collagen fiber, gelatin and two samples of hydrolyzed collagen. The substrates were subjected to individual action of three proteolytic enzymes: papain, bromelain and collagenase (microbial origin). The substrates were incubated in sodium phosphate buffer (0.1 M, pH 7.0) on an orbital shaker at 55°C for different periods of time. In 120 minutes of hydrolysis, the crude collagen fiber showed 37.2% of DH using collagenase, the highest value compared to other substrates. The lowest values for DH were obtained for the hydrolysates collagen, with less than 1% of DH. For hydrolysis in 60 minutes, the DH values were similar to those obtained in 120 minutes of hydrolysis, with minor variations over time. The hydrolytic ability of the collagenase and bromelain was similar and superior compared with the papain. |
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Revista Brasileira de Tecnologia Agroindustrial |
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PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIMEThe interest in collagen use in the food industry to replace synthetic agents is growing every day. Among the derivatives, has the hydrolysate, which dissolves easily in water and brine, and can be incorporated into foods or drinks. The objective of this study was to determine the degree of hydrolysis (DH) of crude collagen fiber, powdered collagen fiber, gelatin and two samples of hydrolyzed collagen. The substrates were subjected to individual action of three proteolytic enzymes: papain, bromelain and collagenase (microbial origin). The substrates were incubated in sodium phosphate buffer (0.1 M, pH 7.0) on an orbital shaker at 55°C for different periods of time. In 120 minutes of hydrolysis, the crude collagen fiber showed 37.2% of DH using collagenase, the highest value compared to other substrates. The lowest values for DH were obtained for the hydrolysates collagen, with less than 1% of DH. For hydrolysis in 60 minutes, the DH values were similar to those obtained in 120 minutes of hydrolysis, with minor variations over time. The hydrolytic ability of the collagenase and bromelain was similar and superior compared with the papain.Universidade Tecnológica Federal do Paraná (UTFPR)Iltchenco, SidianeKempka, Aniela PintoPrestes, Rosa Cristina2017-05-27info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://periodicos.utfpr.edu.br/rbta/article/view/275510.3895/rbta.v11n1.2755Revista Brasileira de Tecnologia Agroindustrial; v. 11, n. 1 (2017)1981-368610.3895/rbta.v11n1reponame:Revista Brasileira de Tecnologia Agroindustrialinstname:Universidade Tecnológica Federal do Paraná (UTFPR)instacron:UTFPRporhttps://periodicos.utfpr.edu.br/rbta/article/view/2755/3705Direitos autorais 2017 CC-BYhttp://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccess2017-06-16T00:01:38Zoai:periodicos.utfpr:article/2755Revistahttps://periodicos.utfpr.edu.br/rbtaPUBhttps://periodicos.utfpr.edu.br/rbta/oai||rbta-pg@utfpr.edu.br1981-36861981-3686opendoar:2017-06-16T00:01:38Revista Brasileira de Tecnologia Agroindustrial - Universidade Tecnológica Federal do Paraná (UTFPR)false |
dc.title.none.fl_str_mv |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME |
title |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME |
spellingShingle |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME Iltchenco, Sidiane |
title_short |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME |
title_full |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME |
title_fullStr |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME |
title_full_unstemmed |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME |
title_sort |
PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME |
author |
Iltchenco, Sidiane |
author_facet |
Iltchenco, Sidiane Kempka, Aniela Pinto Prestes, Rosa Cristina |
author_role |
author |
author2 |
Kempka, Aniela Pinto Prestes, Rosa Cristina |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
|
dc.contributor.author.fl_str_mv |
Iltchenco, Sidiane Kempka, Aniela Pinto Prestes, Rosa Cristina |
dc.subject.none.fl_str_mv |
|
description |
The interest in collagen use in the food industry to replace synthetic agents is growing every day. Among the derivatives, has the hydrolysate, which dissolves easily in water and brine, and can be incorporated into foods or drinks. The objective of this study was to determine the degree of hydrolysis (DH) of crude collagen fiber, powdered collagen fiber, gelatin and two samples of hydrolyzed collagen. The substrates were subjected to individual action of three proteolytic enzymes: papain, bromelain and collagenase (microbial origin). The substrates were incubated in sodium phosphate buffer (0.1 M, pH 7.0) on an orbital shaker at 55°C for different periods of time. In 120 minutes of hydrolysis, the crude collagen fiber showed 37.2% of DH using collagenase, the highest value compared to other substrates. The lowest values for DH were obtained for the hydrolysates collagen, with less than 1% of DH. For hydrolysis in 60 minutes, the DH values were similar to those obtained in 120 minutes of hydrolysis, with minor variations over time. The hydrolytic ability of the collagenase and bromelain was similar and superior compared with the papain. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-05-27 |
dc.type.none.fl_str_mv |
|
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://periodicos.utfpr.edu.br/rbta/article/view/2755 10.3895/rbta.v11n1.2755 |
url |
https://periodicos.utfpr.edu.br/rbta/article/view/2755 |
identifier_str_mv |
10.3895/rbta.v11n1.2755 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
https://periodicos.utfpr.edu.br/rbta/article/view/2755/3705 |
dc.rights.driver.fl_str_mv |
Direitos autorais 2017 CC-BY http://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Direitos autorais 2017 CC-BY http://creativecommons.org/licenses/by/4.0 |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Tecnológica Federal do Paraná (UTFPR) |
publisher.none.fl_str_mv |
Universidade Tecnológica Federal do Paraná (UTFPR) |
dc.source.none.fl_str_mv |
Revista Brasileira de Tecnologia Agroindustrial; v. 11, n. 1 (2017) 1981-3686 10.3895/rbta.v11n1 reponame:Revista Brasileira de Tecnologia Agroindustrial instname:Universidade Tecnológica Federal do Paraná (UTFPR) instacron:UTFPR |
instname_str |
Universidade Tecnológica Federal do Paraná (UTFPR) |
instacron_str |
UTFPR |
institution |
UTFPR |
reponame_str |
Revista Brasileira de Tecnologia Agroindustrial |
collection |
Revista Brasileira de Tecnologia Agroindustrial |
repository.name.fl_str_mv |
Revista Brasileira de Tecnologia Agroindustrial - Universidade Tecnológica Federal do Paraná (UTFPR) |
repository.mail.fl_str_mv |
||rbta-pg@utfpr.edu.br |
_version_ |
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