Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts
Autor(a) principal: | |
---|---|
Data de Publicação: | 2017 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Food Science and Technology (Campinas) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612017000200176 |
Resumo: | Abstract Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin byproducts of paddlefish (ASC-P and PSC-P) and globefish (ASC-G and PSC-G) were purified and characterized. The imino acid contents of ASC-P, PSC-P, ASC-G and PSC-G were 194.1, 197.9, 186.4 and 189.7 residues/1000 residues, respectively. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) confirmed that all four samples composed of two different α1- and α2-chains with integrated triple-helical structure. Denaturation temperatures of ASC-P, PSC-P, ASC-G and PSC-G were 29.6, 28.2, 27.4 and 26.9 °C, respectively. Based on Transmission electron microscopy (TEM) observation, all four samples could assemble into fibrils in vitro with D-periodicity. However, the fibril-forming rate of ASC-P and PSC-P was more rapid than that of ASC-G and PSC-G. Scanning electron microscopy (SEM) analysis confirmed well-defined fibril morphologies,the diameter of fibrils from ASC-P and PSC-P was thicker than those of ASC-G and PSC-G after 24 h incubation. These results indicated that paddlefish and globefish skin collagens could be alternatives to terrestrial collagens for applications in food-packaging, nutraceutical and pharmaceutical industries. |
id |
SBCTA-1_ed31756e6e36925b1006995a0978cc02 |
---|---|
oai_identifier_str |
oai:scielo:S0101-20612017000200176 |
network_acronym_str |
SBCTA-1 |
network_name_str |
Food Science and Technology (Campinas) |
repository_id_str |
|
spelling |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproductspaddlefishglobefishcollagenphysicochemical propertyfibril-forming propertyfibril morphologyAbstract Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin byproducts of paddlefish (ASC-P and PSC-P) and globefish (ASC-G and PSC-G) were purified and characterized. The imino acid contents of ASC-P, PSC-P, ASC-G and PSC-G were 194.1, 197.9, 186.4 and 189.7 residues/1000 residues, respectively. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) confirmed that all four samples composed of two different α1- and α2-chains with integrated triple-helical structure. Denaturation temperatures of ASC-P, PSC-P, ASC-G and PSC-G were 29.6, 28.2, 27.4 and 26.9 °C, respectively. Based on Transmission electron microscopy (TEM) observation, all four samples could assemble into fibrils in vitro with D-periodicity. However, the fibril-forming rate of ASC-P and PSC-P was more rapid than that of ASC-G and PSC-G. Scanning electron microscopy (SEM) analysis confirmed well-defined fibril morphologies,the diameter of fibrils from ASC-P and PSC-P was thicker than those of ASC-G and PSC-G after 24 h incubation. These results indicated that paddlefish and globefish skin collagens could be alternatives to terrestrial collagens for applications in food-packaging, nutraceutical and pharmaceutical industries.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2017-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612017000200176Food Science and Technology v.37 n.2 2017reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/1678-457x.15416info:eu-repo/semantics/openAccessWANG,ShanshanSUN,XiaoqiZHOU,Deqingeng2017-05-24T00:00:00Zoai:scielo:S0101-20612017000200176Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2017-05-24T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts |
title |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts |
spellingShingle |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts WANG,Shanshan paddlefish globefish collagen physicochemical property fibril-forming property fibril morphology |
title_short |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts |
title_full |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts |
title_fullStr |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts |
title_full_unstemmed |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts |
title_sort |
Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts |
author |
WANG,Shanshan |
author_facet |
WANG,Shanshan SUN,Xiaoqi ZHOU,Deqing |
author_role |
author |
author2 |
SUN,Xiaoqi ZHOU,Deqing |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
WANG,Shanshan SUN,Xiaoqi ZHOU,Deqing |
dc.subject.por.fl_str_mv |
paddlefish globefish collagen physicochemical property fibril-forming property fibril morphology |
topic |
paddlefish globefish collagen physicochemical property fibril-forming property fibril morphology |
description |
Abstract Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin byproducts of paddlefish (ASC-P and PSC-P) and globefish (ASC-G and PSC-G) were purified and characterized. The imino acid contents of ASC-P, PSC-P, ASC-G and PSC-G were 194.1, 197.9, 186.4 and 189.7 residues/1000 residues, respectively. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) confirmed that all four samples composed of two different α1- and α2-chains with integrated triple-helical structure. Denaturation temperatures of ASC-P, PSC-P, ASC-G and PSC-G were 29.6, 28.2, 27.4 and 26.9 °C, respectively. Based on Transmission electron microscopy (TEM) observation, all four samples could assemble into fibrils in vitro with D-periodicity. However, the fibril-forming rate of ASC-P and PSC-P was more rapid than that of ASC-G and PSC-G. Scanning electron microscopy (SEM) analysis confirmed well-defined fibril morphologies,the diameter of fibrils from ASC-P and PSC-P was thicker than those of ASC-G and PSC-G after 24 h incubation. These results indicated that paddlefish and globefish skin collagens could be alternatives to terrestrial collagens for applications in food-packaging, nutraceutical and pharmaceutical industries. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-04-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612017000200176 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612017000200176 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/1678-457x.15416 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
dc.source.none.fl_str_mv |
Food Science and Technology v.37 n.2 2017 reponame:Food Science and Technology (Campinas) instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) instacron:SBCTA |
instname_str |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
instacron_str |
SBCTA |
institution |
SBCTA |
reponame_str |
Food Science and Technology (Campinas) |
collection |
Food Science and Technology (Campinas) |
repository.name.fl_str_mv |
Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
repository.mail.fl_str_mv |
||revista@sbcta.org.br |
_version_ |
1752126321696178176 |