Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates

Bioactive peptides were successfully produced from fish (<i>Gadidae</i>) and beef skeletal muscles after being hydrolyzed for 8 h with pepsin. Subsequently, they were purified using a Sep-Pak C18 cartridge and reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular...

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Autores principales:	Mohamed Abdelfattah Maky, Takeshi Zendo
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	bioactive peptides muscle sources pepsin angiotensin-converting enzyme antioxidant antimicrobial peptides Technology T Engineering (General). Civil engineering (General) TA1-2040 Biology (General) QH301-705.5 Physics QC1-999 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/236aabc7184b4e6f9db731c1d0637af5
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spelling	oai:doaj.org-article:236aabc7184b4e6f9db731c1d0637af52021-11-11T15:24:18ZGeneration and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates10.3390/app1121104522076-3417https://doaj.org/article/236aabc7184b4e6f9db731c1d0637af52021-11-01T00:00:00Zhttps://www.mdpi.com/2076-3417/11/21/10452https://doaj.org/toc/2076-3417Bioactive peptides were successfully produced from fish (<i>Gadidae</i>) and beef skeletal muscles after being hydrolyzed for 8 h with pepsin. Subsequently, they were purified using a Sep-Pak C18 cartridge and reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular weights of pure fish and beef peptides were determined to be 2364.4 and 3771.8, respectively. According to Edman degradation, the fish peptide was composed of 21 amino acid residues (F21), while the beef peptide was composed of 34 amino acid residues (B34). F21 and B34 displayed angiotensin-converting enzyme inhibitory activity with a half maximal inhibitory concentration (IC<sub>50</sub>) values of 7.3 µg/mL and 5.8 µg/mL, respectively. F21 exhibited antioxidant activity with an IC<sub>50</sub> value of 389.9 µg/mL, whereas B34 exhibited no antioxidant activity. Moreover, F21 and B34 displayed antimicrobial effects against a wide spectrum of food-borne pathogens and spoilage bacteria. Bioactive peptides derived from muscle proteins are a promising strategy for the production of functional food materials and safe food preservatives.Mohamed Abdelfattah MakyTakeshi ZendoMDPI AGarticlebioactive peptidesmuscle sourcespepsinangiotensin-converting enzymeantioxidantantimicrobial peptidesTechnologyTEngineering (General). Civil engineering (General)TA1-2040Biology (General)QH301-705.5PhysicsQC1-999ChemistryQD1-999ENApplied Sciences, Vol 11, Iss 10452, p 10452 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	bioactive peptides muscle sources pepsin angiotensin-converting enzyme antioxidant antimicrobial peptides Technology T Engineering (General). Civil engineering (General) TA1-2040 Biology (General) QH301-705.5 Physics QC1-999 Chemistry QD1-999
spellingShingle	bioactive peptides muscle sources pepsin angiotensin-converting enzyme antioxidant antimicrobial peptides Technology T Engineering (General). Civil engineering (General) TA1-2040 Biology (General) QH301-705.5 Physics QC1-999 Chemistry QD1-999 Mohamed Abdelfattah Maky Takeshi Zendo Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates
description	Bioactive peptides were successfully produced from fish (<i>Gadidae</i>) and beef skeletal muscles after being hydrolyzed for 8 h with pepsin. Subsequently, they were purified using a Sep-Pak C18 cartridge and reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular weights of pure fish and beef peptides were determined to be 2364.4 and 3771.8, respectively. According to Edman degradation, the fish peptide was composed of 21 amino acid residues (F21), while the beef peptide was composed of 34 amino acid residues (B34). F21 and B34 displayed angiotensin-converting enzyme inhibitory activity with a half maximal inhibitory concentration (IC<sub>50</sub>) values of 7.3 µg/mL and 5.8 µg/mL, respectively. F21 exhibited antioxidant activity with an IC<sub>50</sub> value of 389.9 µg/mL, whereas B34 exhibited no antioxidant activity. Moreover, F21 and B34 displayed antimicrobial effects against a wide spectrum of food-borne pathogens and spoilage bacteria. Bioactive peptides derived from muscle proteins are a promising strategy for the production of functional food materials and safe food preservatives.
format	article
author	Mohamed Abdelfattah Maky Takeshi Zendo
author_facet	Mohamed Abdelfattah Maky Takeshi Zendo
author_sort	Mohamed Abdelfattah Maky
title	Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates
title_short	Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates
title_full	Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates
title_fullStr	Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates
title_full_unstemmed	Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates
title_sort	generation and characterization of novel bioactive peptides from fish and beef hydrolysates
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/236aabc7184b4e6f9db731c1d0637af5
work_keys_str_mv	AT mohamedabdelfattahmaky generationandcharacterizationofnovelbioactivepeptidesfromfishandbeefhydrolysates AT takeshizendo generationandcharacterizationofnovelbioactivepeptidesfromfishandbeefhydrolysates
_version_	1718435355033600000

Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates

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