RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONS
Fish and shrimp industries generate a significant amount of by-products. These by-products can be used for the extraction of enzymes of biomedical interest, such as fibrinolytic and collagenolytic. Thus, this work aimed to perform a screening of fish and shrimp byproducts as sources of enzymes with...
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Instituto de Pesca
2019-02-01
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| Series: | Boletim do Instituto de Pesca |
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| Online Access: | https://institutodepesca.org/index.php/bip/article/view/1340 |
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| author | Vagne de Melo Oliveira Caio Rodrigo Dias Assis Jéssica Costa Silva Quesia Jemima Silva Ranilson de Souza Bezerra Ana Lúcia Figueiredo Porto |
| author_facet | Vagne de Melo Oliveira Caio Rodrigo Dias Assis Jéssica Costa Silva Quesia Jemima Silva Ranilson de Souza Bezerra Ana Lúcia Figueiredo Porto |
| author_sort | Vagne de Melo Oliveira |
| collection | DOAJ |
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Fish and shrimp industries generate a significant amount of by-products. These by-products can be used for the extraction of enzymes of biomedical interest, such as fibrinolytic and collagenolytic. Thus, this work aimed to perform a screening of fish and shrimp byproducts as sources of enzymes with fibrinolytic and collagenolytic activities and to characterize the biochemical properties of crude extracts with collagenolytic activity from Cichla ocellaris residues. Fibrinolytic enzymes were recovered with activities between 5.51 ± 0.02 U.mL-1 (Caranx crysos) and 56.16 ± 0.42 U.mL-1 (Litopenaeus vannamei), while collagenolytic enzymes were detected in a range between 6.79 ± 0.00 U.mg-1 (Trachurus lathami) and 94.35 ± 0.02 U.mg-1 (C. ocellaris). After collagenolytic screening, the selected species was C. ocellaris, being subjected to a preheating, which culminated with an increase of enzymatic activity of 35.07% (up to 127.44 ± 0.09 U.mg-1). The optimal collagenolytic activity recovered from C. ocellaris byproducts was 55 °C (thermostable between 25 and 60 °C) and 7.5 (stable between 6.5 and 11.5) for temperature and pH evaluations, respectively. The kinetic parameters were determined, obtaining Km of 5.92 mM and Vmax of 294.40 U.mg-1. The recovered enzyme was sensitive to the Cu2+, Hg2 and Pb2+ ions, being partially inhibited by phenylmethylsulphonyl fluoride (PMSF), N-p-tosyl-L-lysin chloromethyl ketone (TLCK) and Benzamidine. Furthermore, it was able to cleave native type I collagen, the most important type for industry. Thus, the recovery of biomolecules, besides offering to the industry an alternative source of active molecules, contributes to the reduction of the environmental impact, adding value to the fish product and providing a new source of income.
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| format | Article |
| id | doaj-art-edbeac7c34104f92b9a6b09fdc07aa56 |
| institution | OA Journals |
| issn | 1678-2305 |
| language | English |
| publishDate | 2019-02-01 |
| publisher | Instituto de Pesca |
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| series | Boletim do Instituto de Pesca |
| spelling | doaj-art-edbeac7c34104f92b9a6b09fdc07aa562025-08-20T02:04:33ZengInstituto de PescaBoletim do Instituto de Pesca1678-23052019-02-0145110.20950/1678-2305.2019.45.1.389RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONSVagne de Melo Oliveira0Caio Rodrigo Dias Assis1Jéssica Costa Silva2Quesia Jemima Silva3Ranilson de Souza Bezerra4Ana Lúcia Figueiredo Porto5Universidade Federal Rural de Pernambuco - UFRPE, Laboratório de Tecnologia de Produtos Bioativos - LABTECBIO, Departamento de Morfologia e Fisiologia Animal - DMFA / Universidade Federal de Pernambuco - UFPE, Laboratório de Enzimologia - LABENZ, Departamento de BioquímicaUniversidade Federal de Pernambuco - UFPE, Laboratório de Enzimologia - LABENZ, Departamento de BioquímicaUniversidade Federal Rural de Pernambuco - UFRPE, Laboratório de Tecnologia de Produtos Bioativos - LABTECBIO, Departamento de Morfologia e Fisiologia Animal - DMFAUniversidade Federal Rural de Pernambuco - UFRPE, Laboratório de Tecnologia de Produtos Bioativos - LABTECBIO, Departamento de Morfologia e Fisiologia Animal - DMFAUniversidade Federal de Pernambuco - UFPE, Laboratório de Enzimologia - LABENZ, Departamento de BioquímicaUniversidade Federal Rural de Pernambuco - UFRPE, Laboratório de Tecnologia de Produtos Bioativos - LABTECBIO, Departamento de Morfologia e Fisiologia Animal - DMFA Fish and shrimp industries generate a significant amount of by-products. These by-products can be used for the extraction of enzymes of biomedical interest, such as fibrinolytic and collagenolytic. Thus, this work aimed to perform a screening of fish and shrimp byproducts as sources of enzymes with fibrinolytic and collagenolytic activities and to characterize the biochemical properties of crude extracts with collagenolytic activity from Cichla ocellaris residues. Fibrinolytic enzymes were recovered with activities between 5.51 ± 0.02 U.mL-1 (Caranx crysos) and 56.16 ± 0.42 U.mL-1 (Litopenaeus vannamei), while collagenolytic enzymes were detected in a range between 6.79 ± 0.00 U.mg-1 (Trachurus lathami) and 94.35 ± 0.02 U.mg-1 (C. ocellaris). After collagenolytic screening, the selected species was C. ocellaris, being subjected to a preheating, which culminated with an increase of enzymatic activity of 35.07% (up to 127.44 ± 0.09 U.mg-1). The optimal collagenolytic activity recovered from C. ocellaris byproducts was 55 °C (thermostable between 25 and 60 °C) and 7.5 (stable between 6.5 and 11.5) for temperature and pH evaluations, respectively. The kinetic parameters were determined, obtaining Km of 5.92 mM and Vmax of 294.40 U.mg-1. The recovered enzyme was sensitive to the Cu2+, Hg2 and Pb2+ ions, being partially inhibited by phenylmethylsulphonyl fluoride (PMSF), N-p-tosyl-L-lysin chloromethyl ketone (TLCK) and Benzamidine. Furthermore, it was able to cleave native type I collagen, the most important type for industry. Thus, the recovery of biomolecules, besides offering to the industry an alternative source of active molecules, contributes to the reduction of the environmental impact, adding value to the fish product and providing a new source of income. https://institutodepesca.org/index.php/bip/article/view/1340byproductscollagenasethrombolytic |
| spellingShingle | Vagne de Melo Oliveira Caio Rodrigo Dias Assis Jéssica Costa Silva Quesia Jemima Silva Ranilson de Souza Bezerra Ana Lúcia Figueiredo Porto RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONS Boletim do Instituto de Pesca byproducts collagenase thrombolytic |
| title | RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONS |
| title_full | RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONS |
| title_fullStr | RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONS |
| title_full_unstemmed | RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONS |
| title_short | RECOVERY OF FIBRINOLYTIC AND COLLAGENOLYTIC ENZYMES FROM FISH AND SHRIMP BYPRODUCTS: POTENTIAL SOURCE FOR BIOMEDICAL APPLICATIONS |
| title_sort | recovery of fibrinolytic and collagenolytic enzymes from fish and shrimp byproducts potential source for biomedical applications |
| topic | byproducts collagenase thrombolytic |
| url | https://institutodepesca.org/index.php/bip/article/view/1340 |
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