Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects
Main Author: | |
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Publication Date: | 2023 |
Other Authors: | , , , |
Format: | Article |
Language: | eng |
Source: | Brazilian Journal of Pharmaceutical Sciences |
DOI: | 10.1590/s2175-97902022e201004 |
Download full: | https://www.revistas.usp.br/bjps/article/view/207295 |
Summary: | Serrapeptase, a proteolytic enzyme, has been used for the adjuvant treatment of many diseases. However, its fibrinolytic activity is still uncertain. Herein, the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects were investigated. The results showed that the fibrinolytic activity of serrapeptase was 1295 U/mg, and the specific activity was 3867 U/mg of protein when its proteolytic activity toward casein was 2800 U/mg. The optimum temperature and pH for serrapeptase activity were 37-40°C and 9.0, respectively. At 1 mmol/L, Zn2+, Mn2+ and Fe2+ could activate the fibrinolytic activity of serrapeptase, while K+, Cu2+, sodium dodecyl sulfate (SDS) and ethylene diamine tetraacetic acid (EDTA) inhibited it. In vitro tests showed that serrapeptase could completely prevent blood coagulation at 150 U/mL, and the percentage of blood clot lysis reached 96.6% at 37°C after 4 h at 300 U/mL. These results indicate that serrapeptase has excellent fibrinolytic activity, and can be used as a health food or candidate drug for the prevention or treatment of thrombotic diseases. |
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Brazilian Journal of Pharmaceutical Sciences |
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Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effectsSerrapeptaseProteaseFibrinolytic activityIn vitro thrombolysisSerrapeptase, a proteolytic enzyme, has been used for the adjuvant treatment of many diseases. However, its fibrinolytic activity is still uncertain. Herein, the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects were investigated. The results showed that the fibrinolytic activity of serrapeptase was 1295 U/mg, and the specific activity was 3867 U/mg of protein when its proteolytic activity toward casein was 2800 U/mg. The optimum temperature and pH for serrapeptase activity were 37-40°C and 9.0, respectively. At 1 mmol/L, Zn2+, Mn2+ and Fe2+ could activate the fibrinolytic activity of serrapeptase, while K+, Cu2+, sodium dodecyl sulfate (SDS) and ethylene diamine tetraacetic acid (EDTA) inhibited it. In vitro tests showed that serrapeptase could completely prevent blood coagulation at 150 U/mL, and the percentage of blood clot lysis reached 96.6% at 37°C after 4 h at 300 U/mL. These results indicate that serrapeptase has excellent fibrinolytic activity, and can be used as a health food or candidate drug for the prevention or treatment of thrombotic diseases.Universidade de São Paulo. Faculdade de Ciências Farmacêuticas2023-01-27info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://www.revistas.usp.br/bjps/article/view/20729510.1590/s2175-97902022e201004Brazilian Journal of Pharmaceutical Sciences; Vol. 58 (2022)Brazilian Journal of Pharmaceutical Sciences; v. 58 (2022)Brazilian Journal of Pharmaceutical Sciences; Vol. 58 (2022)2175-97901984-8250reponame:Brazilian Journal of Pharmaceutical Sciencesinstname:Universidade de São Paulo (USP)instacron:USPenghttps://www.revistas.usp.br/bjps/article/view/207295/197590Copyright (c) 2022 Brazilian Journal of Pharmaceutical Scienceshttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessJian feng MeiShao fen CaiYu YiXu dong WangGuo qing Ying2023-08-28T19:22:20Zoai:revistas.usp.br:article/207295Revistahttps://www.revistas.usp.br/bjps/indexPUBhttps://old.scielo.br/oai/scielo-oai.phpbjps@usp.br||elizabeth.igne@gmail.com2175-97901984-8250opendoar:2023-08-28T19:22:20Brazilian Journal of Pharmaceutical Sciences - Universidade de São Paulo (USP)false |
dc.title.none.fl_str_mv |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects |
title |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects |
spellingShingle |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects Jian feng Mei Serrapeptase Protease Fibrinolytic activity In vitro thrombolysis Jian feng Mei Serrapeptase Protease Fibrinolytic activity In vitro thrombolysis |
title_short |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects |
title_full |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects |
title_fullStr |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects |
title_full_unstemmed |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects |
title_sort |
Study of the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects |
author |
Jian feng Mei |
author_facet |
Jian feng Mei Jian feng Mei Shao fen Cai Yu Yi Xu dong Wang Guo qing Ying Shao fen Cai Yu Yi Xu dong Wang Guo qing Ying |
author_role |
author |
author2 |
Shao fen Cai Yu Yi Xu dong Wang Guo qing Ying |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Jian feng Mei Shao fen Cai Yu Yi Xu dong Wang Guo qing Ying |
dc.subject.por.fl_str_mv |
Serrapeptase Protease Fibrinolytic activity In vitro thrombolysis |
topic |
Serrapeptase Protease Fibrinolytic activity In vitro thrombolysis |
description |
Serrapeptase, a proteolytic enzyme, has been used for the adjuvant treatment of many diseases. However, its fibrinolytic activity is still uncertain. Herein, the fibrinolytic activity of serrapeptase and its in vitro thrombolytic effects were investigated. The results showed that the fibrinolytic activity of serrapeptase was 1295 U/mg, and the specific activity was 3867 U/mg of protein when its proteolytic activity toward casein was 2800 U/mg. The optimum temperature and pH for serrapeptase activity were 37-40°C and 9.0, respectively. At 1 mmol/L, Zn2+, Mn2+ and Fe2+ could activate the fibrinolytic activity of serrapeptase, while K+, Cu2+, sodium dodecyl sulfate (SDS) and ethylene diamine tetraacetic acid (EDTA) inhibited it. In vitro tests showed that serrapeptase could completely prevent blood coagulation at 150 U/mL, and the percentage of blood clot lysis reached 96.6% at 37°C after 4 h at 300 U/mL. These results indicate that serrapeptase has excellent fibrinolytic activity, and can be used as a health food or candidate drug for the prevention or treatment of thrombotic diseases. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-01-27 |
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://www.revistas.usp.br/bjps/article/view/207295 10.1590/s2175-97902022e201004 |
url |
https://www.revistas.usp.br/bjps/article/view/207295 |
identifier_str_mv |
10.1590/s2175-97902022e201004 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
https://www.revistas.usp.br/bjps/article/view/207295/197590 |
dc.rights.driver.fl_str_mv |
Copyright (c) 2022 Brazilian Journal of Pharmaceutical Sciences https://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Copyright (c) 2022 Brazilian Journal of Pharmaceutical Sciences https://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 de São Paulo. Faculdade de Ciências Farmacêuticas |
publisher.none.fl_str_mv |
Universidade de São Paulo. Faculdade de Ciências Farmacêuticas |
dc.source.none.fl_str_mv |
Brazilian Journal of Pharmaceutical Sciences; Vol. 58 (2022) Brazilian Journal of Pharmaceutical Sciences; v. 58 (2022) Brazilian Journal of Pharmaceutical Sciences; Vol. 58 (2022) 2175-9790 1984-8250 reponame:Brazilian Journal of Pharmaceutical Sciences instname:Universidade de São Paulo (USP) instacron:USP |
instname_str |
Universidade de São Paulo (USP) |
instacron_str |
USP |
institution |
USP |
reponame_str |
Brazilian Journal of Pharmaceutical Sciences |
collection |
Brazilian Journal of Pharmaceutical Sciences |
repository.name.fl_str_mv |
Brazilian Journal of Pharmaceutical Sciences - Universidade de São Paulo (USP) |
repository.mail.fl_str_mv |
bjps@usp.br||elizabeth.igne@gmail.com |
_version_ |
1822179249925128192 |
dc.identifier.doi.none.fl_str_mv |
10.1590/s2175-97902022e201004 |