Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates
Autor(a) principal: | |
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Data de Publicação: | 2020 |
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=S0101-20612020000500287 |
Resumo: | Abstract Protepsin belongs to the class of acid proteinases, containing carboxyl groups in the active center. The preparation cleaves peptide bonds formed by aromatic amino acids (tyrosine, phenylalanine), and does not hydrolize esters and amides. Along with the proteolytic complex, Protepsin contains collagenase, lipase, and other digestive enzymes. The preparation is obtained according to the original technology through maceration of animal endocrine raw materials, followed by purification, concentration, isolation and freeze dehydration of the enzyme complex. The results of the laboratory studies of the proteolytic activity of enzyme preparations show that Protepsin, the preparation of animal origin with a proteolytic activity of 100 units/g, has the greatest collagenase activity in the biomodification of native collagen-containing raw materials. |
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Food Science and Technology (Campinas) |
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Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzatesenzyme preparationsProtepsincattle by-productsproteolytic activityprotein hydrolysateAbstract Protepsin belongs to the class of acid proteinases, containing carboxyl groups in the active center. The preparation cleaves peptide bonds formed by aromatic amino acids (tyrosine, phenylalanine), and does not hydrolize esters and amides. Along with the proteolytic complex, Protepsin contains collagenase, lipase, and other digestive enzymes. The preparation is obtained according to the original technology through maceration of animal endocrine raw materials, followed by purification, concentration, isolation and freeze dehydration of the enzyme complex. The results of the laboratory studies of the proteolytic activity of enzyme preparations show that Protepsin, the preparation of animal origin with a proteolytic activity of 100 units/g, has the greatest collagenase activity in the biomodification of native collagen-containing raw materials.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2020-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612020000500287Food Science and Technology v.40 suppl.1 2020reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.09319info:eu-repo/semantics/openAccessLUKIN,Aleksandreng2020-06-24T00:00:00Zoai:scielo:S0101-20612020000500287Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2020-06-24T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates |
title |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates |
spellingShingle |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates LUKIN,Aleksandr enzyme preparations Protepsin cattle by-products proteolytic activity protein hydrolysate |
title_short |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates |
title_full |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates |
title_fullStr |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates |
title_full_unstemmed |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates |
title_sort |
Application and comparison of proteolytic enzyme preparations in technology of protein hydrolyzates |
author |
LUKIN,Aleksandr |
author_facet |
LUKIN,Aleksandr |
author_role |
author |
dc.contributor.author.fl_str_mv |
LUKIN,Aleksandr |
dc.subject.por.fl_str_mv |
enzyme preparations Protepsin cattle by-products proteolytic activity protein hydrolysate |
topic |
enzyme preparations Protepsin cattle by-products proteolytic activity protein hydrolysate |
description |
Abstract Protepsin belongs to the class of acid proteinases, containing carboxyl groups in the active center. The preparation cleaves peptide bonds formed by aromatic amino acids (tyrosine, phenylalanine), and does not hydrolize esters and amides. Along with the proteolytic complex, Protepsin contains collagenase, lipase, and other digestive enzymes. The preparation is obtained according to the original technology through maceration of animal endocrine raw materials, followed by purification, concentration, isolation and freeze dehydration of the enzyme complex. The results of the laboratory studies of the proteolytic activity of enzyme preparations show that Protepsin, the preparation of animal origin with a proteolytic activity of 100 units/g, has the greatest collagenase activity in the biomodification of native collagen-containing raw materials. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-06-01 |
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=S0101-20612020000500287 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612020000500287 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/fst.09319 |
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.40 suppl.1 2020 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_ |
1752126326357098496 |