Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat

Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Nabila Begum [verfasserIn] Qudrat Ullah Khan [verfasserIn] Sam Al-Dalali [verfasserIn] Daoqiang Lu [verfasserIn] Fang Yang [verfasserIn] Jie Li [verfasserIn] Di Wu [verfasserIn] Riwang Li [verfasserIn] Jun Wang [verfasserIn] Dahai Liu [verfasserIn] Huanlu Song [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2024

Schlagwörter:	cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity

Übergeordnetes Werk:	In: Frontiers in Sustainable Food Systems - Frontiers Media S.A., 2018, 7(2024)
Übergeordnetes Werk:	volume:7 ; year:2024

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fsufs.2023.1345833

Katalog-ID:	DOAJ094738513

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allfields	10.3389/fsufs.2023.1345833 doi (DE-627)DOAJ094738513 (DE-599)DOAJc04368e4a75e4793ae3cc61e17047b2f DE-627 ger DE-627 rakwb eng TX341-641 TP368-456 Nabila Begum verfasserin aut Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry. cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity Nutrition. Foods and food supply Food processing and manufacture Nabila Begum verfasserin aut Qudrat Ullah Khan verfasserin aut Sam Al-Dalali verfasserin aut Daoqiang Lu verfasserin aut Fang Yang verfasserin aut Jie Li verfasserin aut Di Wu verfasserin aut Riwang Li verfasserin aut Jun Wang verfasserin aut Dahai Liu verfasserin aut Huanlu Song verfasserin aut In Frontiers in Sustainable Food Systems Frontiers Media S.A., 2018 7(2024) (DE-627)1019902493 (DE-600)2928540-9 2571581X nnns volume:7 year:2024 https://doi.org/10.3389/fsufs.2023.1345833 kostenfrei https://doaj.org/article/c04368e4a75e4793ae3cc61e17047b2f kostenfrei https://www.frontiersin.org/articles/10.3389/fsufs.2023.1345833/full kostenfrei https://doaj.org/toc/2571-581X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 7 2024
spelling	10.3389/fsufs.2023.1345833 doi (DE-627)DOAJ094738513 (DE-599)DOAJc04368e4a75e4793ae3cc61e17047b2f DE-627 ger DE-627 rakwb eng TX341-641 TP368-456 Nabila Begum verfasserin aut Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry. cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity Nutrition. Foods and food supply Food processing and manufacture Nabila Begum verfasserin aut Qudrat Ullah Khan verfasserin aut Sam Al-Dalali verfasserin aut Daoqiang Lu verfasserin aut Fang Yang verfasserin aut Jie Li verfasserin aut Di Wu verfasserin aut Riwang Li verfasserin aut Jun Wang verfasserin aut Dahai Liu verfasserin aut Huanlu Song verfasserin aut In Frontiers in Sustainable Food Systems Frontiers Media S.A., 2018 7(2024) (DE-627)1019902493 (DE-600)2928540-9 2571581X nnns volume:7 year:2024 https://doi.org/10.3389/fsufs.2023.1345833 kostenfrei https://doaj.org/article/c04368e4a75e4793ae3cc61e17047b2f kostenfrei https://www.frontiersin.org/articles/10.3389/fsufs.2023.1345833/full kostenfrei https://doaj.org/toc/2571-581X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 7 2024
allfields_unstemmed	10.3389/fsufs.2023.1345833 doi (DE-627)DOAJ094738513 (DE-599)DOAJc04368e4a75e4793ae3cc61e17047b2f DE-627 ger DE-627 rakwb eng TX341-641 TP368-456 Nabila Begum verfasserin aut Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry. cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity Nutrition. Foods and food supply Food processing and manufacture Nabila Begum verfasserin aut Qudrat Ullah Khan verfasserin aut Sam Al-Dalali verfasserin aut Daoqiang Lu verfasserin aut Fang Yang verfasserin aut Jie Li verfasserin aut Di Wu verfasserin aut Riwang Li verfasserin aut Jun Wang verfasserin aut Dahai Liu verfasserin aut Huanlu Song verfasserin aut In Frontiers in Sustainable Food Systems Frontiers Media S.A., 2018 7(2024) (DE-627)1019902493 (DE-600)2928540-9 2571581X nnns volume:7 year:2024 https://doi.org/10.3389/fsufs.2023.1345833 kostenfrei https://doaj.org/article/c04368e4a75e4793ae3cc61e17047b2f kostenfrei https://www.frontiersin.org/articles/10.3389/fsufs.2023.1345833/full kostenfrei https://doaj.org/toc/2571-581X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 7 2024
allfieldsGer	10.3389/fsufs.2023.1345833 doi (DE-627)DOAJ094738513 (DE-599)DOAJc04368e4a75e4793ae3cc61e17047b2f DE-627 ger DE-627 rakwb eng TX341-641 TP368-456 Nabila Begum verfasserin aut Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry. cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity Nutrition. Foods and food supply Food processing and manufacture Nabila Begum verfasserin aut Qudrat Ullah Khan verfasserin aut Sam Al-Dalali verfasserin aut Daoqiang Lu verfasserin aut Fang Yang verfasserin aut Jie Li verfasserin aut Di Wu verfasserin aut Riwang Li verfasserin aut Jun Wang verfasserin aut Dahai Liu verfasserin aut Huanlu Song verfasserin aut In Frontiers in Sustainable Food Systems Frontiers Media S.A., 2018 7(2024) (DE-627)1019902493 (DE-600)2928540-9 2571581X nnns volume:7 year:2024 https://doi.org/10.3389/fsufs.2023.1345833 kostenfrei https://doaj.org/article/c04368e4a75e4793ae3cc61e17047b2f kostenfrei https://www.frontiersin.org/articles/10.3389/fsufs.2023.1345833/full kostenfrei https://doaj.org/toc/2571-581X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 7 2024
allfieldsSound	10.3389/fsufs.2023.1345833 doi (DE-627)DOAJ094738513 (DE-599)DOAJc04368e4a75e4793ae3cc61e17047b2f DE-627 ger DE-627 rakwb eng TX341-641 TP368-456 Nabila Begum verfasserin aut Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry. cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity Nutrition. Foods and food supply Food processing and manufacture Nabila Begum verfasserin aut Qudrat Ullah Khan verfasserin aut Sam Al-Dalali verfasserin aut Daoqiang Lu verfasserin aut Fang Yang verfasserin aut Jie Li verfasserin aut Di Wu verfasserin aut Riwang Li verfasserin aut Jun Wang verfasserin aut Dahai Liu verfasserin aut Huanlu Song verfasserin aut In Frontiers in Sustainable Food Systems Frontiers Media S.A., 2018 7(2024) (DE-627)1019902493 (DE-600)2928540-9 2571581X nnns volume:7 year:2024 https://doi.org/10.3389/fsufs.2023.1345833 kostenfrei https://doaj.org/article/c04368e4a75e4793ae3cc61e17047b2f kostenfrei https://www.frontiersin.org/articles/10.3389/fsufs.2023.1345833/full kostenfrei https://doaj.org/toc/2571-581X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 7 2024
language	English
source	In Frontiers in Sustainable Food Systems 7(2024) volume:7 year:2024
sourceStr	In Frontiers in Sustainable Food Systems 7(2024) volume:7 year:2024
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity Nutrition. Foods and food supply Food processing and manufacture
isfreeaccess_bool	true
container_title	Frontiers in Sustainable Food Systems
authorswithroles_txt_mv	Nabila Begum @@aut@@ Qudrat Ullah Khan @@aut@@ Sam Al-Dalali @@aut@@ Daoqiang Lu @@aut@@ Fang Yang @@aut@@ Jie Li @@aut@@ Di Wu @@aut@@ Riwang Li @@aut@@ Jun Wang @@aut@@ Dahai Liu @@aut@@ Huanlu Song @@aut@@
publishDateDaySort_date	2024-01-01T00:00:00Z
hierarchy_top_id	1019902493
id	DOAJ094738513
language_de	englisch
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These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). 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callnumber-first	T - Technology
author	Nabila Begum
spellingShingle	Nabila Begum misc TX341-641 misc TP368-456 misc cultured meat misc enzymatic hydrolysate misc ultrafiltration misc antioxidant capacity misc chromatography misc hydrophobicity misc Nutrition. Foods and food supply misc Food processing and manufacture Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat
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topic_title	TX341-641 TP368-456 Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat cultured meat enzymatic hydrolysate ultrafiltration antioxidant capacity chromatography hydrophobicity
topic	misc TX341-641 misc TP368-456 misc cultured meat misc enzymatic hydrolysate misc ultrafiltration misc antioxidant capacity misc chromatography misc hydrophobicity misc Nutrition. Foods and food supply misc Food processing and manufacture
topic_unstemmed	misc TX341-641 misc TP368-456 misc cultured meat misc enzymatic hydrolysate misc ultrafiltration misc antioxidant capacity misc chromatography misc hydrophobicity misc Nutrition. Foods and food supply misc Food processing and manufacture
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title	Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat
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title_full	Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat
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author_browse	Nabila Begum Qudrat Ullah Khan Sam Al-Dalali Daoqiang Lu Fang Yang Jie Li Di Wu Riwang Li Jun Wang Dahai Liu Huanlu Song
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title_sort	process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat
callnumber	TX341-641
title_auth	Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat
abstract	Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry.
abstractGer	Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry.
abstract_unstemmed	Bone protein is a significant secondary product of the meat industry, comprising a substantial quantity of protein. These proteins could be broken down through enzymatic hydrolysis to generate antioxidant peptides. This study aimed to produce antioxidant peptides from bovine bone extract by enzymatic hydrolysis utilizing Flavourzyme and Protamex by optimizing enzyme amounts and time using the Box–Behnken design. The final optimized conditions obtained through the model were as follows: The amount of Flavourzyme was 1,100 U, the amount of Protamex was 2,814 U, and the time was 3.77 (h). Bovine bone extract hydrolysate (BBEH) was purified stepwise using ultrafiltration membranes with molecular cutoffs of 5, 3, and 1 kDa. To assess the antioxidant capacity of the fractions, several methods were used, including radical scavenging activity “1,1-diphenyl-2-picrylhydrazyl (DPPH),” “2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS),” metal chelating activity (MCA), reducing power (RP), and thiobarbituric acid assay (TBA). The results indicated that the ultrafiltration fraction with a molecular weight of less than 1 kDa showed significant antioxidant activity, with 48, 42, and 50% inhibition rates for DPPH, ABTS, and metal chelating, respectively. Using size exclusion chromatography, the fraction with a molecular weight less than 1 kDa was further separated into five sub-fractions: Frac-I, Frac-II, Frac-III, Frac-IV, and Frac-V. Sub-Frac-III, which exhibits significant DPPH radical scavenging activity (55%) and a reducing power of 0.8 at 700 nm, was separated into six sub-sub-fractions using reversed-phase HPLC (RP-HPLC) based on molecular weight and hydrophobicity. The sub-sub-fraction with the highest value for DPPH radical scavenging activity was sub-Fra-III-6, which exhibited approximately 69.45% activity. The sub-Fra-III-6 was analyzed using LC–MS/MS, which identified two specific peptides: Ala-Pro-Phe with a mass of 333.12 Da and Asp-His-Val with a mass of 369.14 Da. These two peptides are likely the primary peptides that might have a crucial role in antioxidant capacity. It can be concluded that BBEH is a valuable source of natural antioxidants and has the potential to serve as a viable resource in the cultured meat industry.
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title_short	Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat
url	https://doi.org/10.3389/fsufs.2023.1345833 https://doaj.org/article/c04368e4a75e4793ae3cc61e17047b2f https://www.frontiersin.org/articles/10.3389/fsufs.2023.1345833/full https://doaj.org/toc/2571-581X
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Process optimization and identification of antioxidant peptides from enzymatic hydrolysate of bovine bone extract, a potential source in cultured meat

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