Feather Meal as a Source of Peptides with Antioxidant Activity from Enzymatic Hydrolysis
Feather is the most abundant keratinous material in nature. This by-product of animal origin has about 80–90% of crude protein. This work aimed to maximize the enzymatic hydrolysis of feather meal using the proteolytic enzyme from Bacillus sp. P45 and evaluate the antioxidant capacity of different f...
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| Veröffentlicht in: | Waste and biomass valorization 2023-02, Vol.14 (2), p.421-430 |
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| creator | da Cunha, Igreine Couto Brandelli, Adriano Braga, Anna Rafaela Cavalcante Sala, Luisa Kalil, Susana Juliano |
| description | Feather is the most abundant keratinous material in nature. This by-product of animal origin has about 80–90% of crude protein. This work aimed to maximize the enzymatic hydrolysis of feather meal using the proteolytic enzyme from
Bacillus
sp. P45 and evaluate the antioxidant capacity of different fractions of the hydrolysate. Enzymatic hydrolysis was maximized using a central composite rotatable design (CCRD) 2
4
, where the effects of the variables CaCl
2
concentration (0–100 mmol/L), temperature (35–55 °C), enzyme/substrate ratio (600–6000 U/g-protein), and substrate protein concentration (10–40 g/L) were estimated on the responses degree of hydrolysis (DH) and protein recovery (PR). The highest values of DH and PR were obtained when the hydrolysis was performed with 50 mmol/L of CaCl
2
, 50 °C, 6000 U/g-protein, and substrate protein concentration of 10 g/L. Hydrolysate presented DH of 8.4% and PR of 37.5% at 6 h of reaction. The obtained peptides were separated by molecular weight through a sequential ultrafiltration process in the membranes of 10 and 3 kDa, and the antioxidant activities of the different fractions were analyzed. The fraction |
| doi_str_mv | 10.1007/s12649-022-01886-8 |
| format | Article |
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Bacillus
sp. P45 and evaluate the antioxidant capacity of different fractions of the hydrolysate. Enzymatic hydrolysis was maximized using a central composite rotatable design (CCRD) 2
4
, where the effects of the variables CaCl
2
concentration (0–100 mmol/L), temperature (35–55 °C), enzyme/substrate ratio (600–6000 U/g-protein), and substrate protein concentration (10–40 g/L) were estimated on the responses degree of hydrolysis (DH) and protein recovery (PR). The highest values of DH and PR were obtained when the hydrolysis was performed with 50 mmol/L of CaCl
2
, 50 °C, 6000 U/g-protein, and substrate protein concentration of 10 g/L. Hydrolysate presented DH of 8.4% and PR of 37.5% at 6 h of reaction. The obtained peptides were separated by molecular weight through a sequential ultrafiltration process in the membranes of 10 and 3 kDa, and the antioxidant activities of the different fractions were analyzed. The fraction < 3 kDa showed a higher capacity to sequester radicals ABTS
⋅+
(90.20 μmol TE/g) and peroxyl (1892.47 μmol TE/g). This study shows the potential of
Bacillus
sp. P45 in hydrolyzing feather meal, resulting in peptides with antioxidant activity.
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Bacillus
sp. P45 and evaluate the antioxidant capacity of different fractions of the hydrolysate. Enzymatic hydrolysis was maximized using a central composite rotatable design (CCRD) 2
4
, where the effects of the variables CaCl
2
concentration (0–100 mmol/L), temperature (35–55 °C), enzyme/substrate ratio (600–6000 U/g-protein), and substrate protein concentration (10–40 g/L) were estimated on the responses degree of hydrolysis (DH) and protein recovery (PR). The highest values of DH and PR were obtained when the hydrolysis was performed with 50 mmol/L of CaCl
2
, 50 °C, 6000 U/g-protein, and substrate protein concentration of 10 g/L. Hydrolysate presented DH of 8.4% and PR of 37.5% at 6 h of reaction. The obtained peptides were separated by molecular weight through a sequential ultrafiltration process in the membranes of 10 and 3 kDa, and the antioxidant activities of the different fractions were analyzed. The fraction < 3 kDa showed a higher capacity to sequester radicals ABTS
⋅+
(90.20 μmol TE/g) and peroxyl (1892.47 μmol TE/g). This study shows the potential of
Bacillus
sp. P45 in hydrolyzing feather meal, resulting in peptides with antioxidant activity.
Graphical Abstract</description><subject>Antioxidants</subject><subject>Bacillus</subject><subject>Calcium chloride</subject><subject>Engineering</subject><subject>Environment</subject><subject>Environmental Engineering/Biotechnology</subject><subject>Enzymes</subject><subject>Feathers</subject><subject>Hydrolysates</subject><subject>Hydrolysis</subject><subject>Industrial Pollution Prevention</subject><subject>Molecular weight</subject><subject>Original Paper</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Renewable and Green Energy</subject><subject>Substrates</subject><subject>Ultrafiltration</subject><subject>Waste Management/Waste Technology</subject><issn>1877-2641</issn><issn>1877-265X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9kE1Lw0AQhhdRsNT-AU8LnqP7ld3NsZTWChUFFXpbNsnEbmmTuLtV4683GtGbp5nD-7wzPAidU3JJCVFXgTIpsoQwlhCqtUz0ERpRrVTCZLo-_t0FPUWTELaEEEapZlyN0HoBNm7A41uwO2wDtvihOfgCcFPhe2ijKyHgNxc3eFpH17y70tYRT4voXl3scOWbPZ7XH93eRlfgZVf6ZtcFF87QSWV3ASY_c4yeFvPH2TJZ3V3fzKarpGAiiwnPgMuSCllKpajOpdKapLYSKS0FZ2meZ0KxSuVS6CJNScVTBhQYqCyHXBd8jC6G3tY3LwcI0Wz7_-v-pGF9I5dSc9qn2JAqfBOCh8q03u2t7wwl5kuiGSSaXqL5lmh0D_EBCn24fgb_V_0P9QmZxnPn</recordid><startdate>20230201</startdate><enddate>20230201</enddate><creator>da Cunha, Igreine Couto</creator><creator>Brandelli, Adriano</creator><creator>Braga, Anna Rafaela Cavalcante</creator><creator>Sala, Luisa</creator><creator>Kalil, Susana Juliano</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0002-7052-0226</orcidid><orcidid>https://orcid.org/0000-0003-3517-0926</orcidid><orcidid>https://orcid.org/0000-0002-9307-6471</orcidid><orcidid>https://orcid.org/0000-0001-5548-5744</orcidid><orcidid>https://orcid.org/0000-0001-8132-2033</orcidid></search><sort><creationdate>20230201</creationdate><title>Feather Meal as a Source of Peptides with Antioxidant Activity from Enzymatic Hydrolysis</title><author>da Cunha, Igreine Couto ; Brandelli, Adriano ; Braga, Anna Rafaela Cavalcante ; Sala, Luisa ; Kalil, Susana Juliano</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c249t-39e36d146d67718b678805af451d4325bb9472f7b648c550f352e1e2e79beb8c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Antioxidants</topic><topic>Bacillus</topic><topic>Calcium chloride</topic><topic>Engineering</topic><topic>Environment</topic><topic>Environmental Engineering/Biotechnology</topic><topic>Enzymes</topic><topic>Feathers</topic><topic>Hydrolysates</topic><topic>Hydrolysis</topic><topic>Industrial Pollution Prevention</topic><topic>Molecular weight</topic><topic>Original Paper</topic><topic>Peptides</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Renewable and Green Energy</topic><topic>Substrates</topic><topic>Ultrafiltration</topic><topic>Waste Management/Waste Technology</topic><toplevel>online_resources</toplevel><creatorcontrib>da Cunha, Igreine Couto</creatorcontrib><creatorcontrib>Brandelli, Adriano</creatorcontrib><creatorcontrib>Braga, Anna Rafaela Cavalcante</creatorcontrib><creatorcontrib>Sala, Luisa</creatorcontrib><creatorcontrib>Kalil, Susana Juliano</creatorcontrib><collection>CrossRef</collection><jtitle>Waste and biomass valorization</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>da Cunha, Igreine Couto</au><au>Brandelli, Adriano</au><au>Braga, Anna Rafaela Cavalcante</au><au>Sala, Luisa</au><au>Kalil, Susana Juliano</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Feather Meal as a Source of Peptides with Antioxidant Activity from Enzymatic Hydrolysis</atitle><jtitle>Waste and biomass valorization</jtitle><stitle>Waste Biomass Valor</stitle><date>2023-02-01</date><risdate>2023</risdate><volume>14</volume><issue>2</issue><spage>421</spage><epage>430</epage><pages>421-430</pages><issn>1877-2641</issn><eissn>1877-265X</eissn><abstract>Feather is the most abundant keratinous material in nature. This by-product of animal origin has about 80–90% of crude protein. This work aimed to maximize the enzymatic hydrolysis of feather meal using the proteolytic enzyme from
Bacillus
sp. P45 and evaluate the antioxidant capacity of different fractions of the hydrolysate. Enzymatic hydrolysis was maximized using a central composite rotatable design (CCRD) 2
4
, where the effects of the variables CaCl
2
concentration (0–100 mmol/L), temperature (35–55 °C), enzyme/substrate ratio (600–6000 U/g-protein), and substrate protein concentration (10–40 g/L) were estimated on the responses degree of hydrolysis (DH) and protein recovery (PR). The highest values of DH and PR were obtained when the hydrolysis was performed with 50 mmol/L of CaCl
2
, 50 °C, 6000 U/g-protein, and substrate protein concentration of 10 g/L. Hydrolysate presented DH of 8.4% and PR of 37.5% at 6 h of reaction. The obtained peptides were separated by molecular weight through a sequential ultrafiltration process in the membranes of 10 and 3 kDa, and the antioxidant activities of the different fractions were analyzed. The fraction < 3 kDa showed a higher capacity to sequester radicals ABTS
⋅+
(90.20 μmol TE/g) and peroxyl (1892.47 μmol TE/g). This study shows the potential of
Bacillus
sp. P45 in hydrolyzing feather meal, resulting in peptides with antioxidant activity.
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| subjects | Antioxidants Bacillus Calcium chloride Engineering Environment Environmental Engineering/Biotechnology Enzymes Feathers Hydrolysates Hydrolysis Industrial Pollution Prevention Molecular weight Original Paper Peptides Proteins Proteolysis Renewable and Green Energy Substrates Ultrafiltration Waste Management/Waste Technology |
| title | Feather Meal as a Source of Peptides with Antioxidant Activity from Enzymatic Hydrolysis |
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