From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L
The valorization of fishery byproducts is essential to reduce waste and create high-value products. Waste from Argentine hake (Merluccius hubbsi) could enhance its functional and antioxidant properties through hydrolysis, releasing peptides with bioactive properties. Protein hydrolysates of Argenti...
Saved in:
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Instituto Nacional de Investigación y Desarrollo Pesquero (INIDEP)
2025-01-01
|
| Series: | Marine and Fishery Sciences |
| Subjects: | |
| Online Access: | https://ojs.inidep.edu.ar/index.php/mafis/article/view/403 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1841533381672697856 |
|---|---|
| author | Clara Liebana Nair de los Ángeles Pereira Analia Fernández-Gimenez Maria Florencia Fangio |
| author_facet | Clara Liebana Nair de los Ángeles Pereira Analia Fernández-Gimenez Maria Florencia Fangio |
| author_sort | Clara Liebana |
| collection | DOAJ |
| description |
The valorization of fishery byproducts is essential to reduce waste and create high-value products. Waste from Argentine hake (Merluccius hubbsi) could enhance its functional and antioxidant properties through hydrolysis, releasing peptides with bioactive properties. Protein hydrolysates of Argentine hake were produced through autolysis (Aut) and enzymatic hydrolysis using Alcalase® 2.4L at concentrations of 0.24% and 2% (v/v) (Alc-0.24 and Alc-2), respectively, over 150 min. Alkaline peptidase activity, degree of hydrolysis, and antioxidant activity were assessed using 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2’-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) radical ABTS·+ scavenging assays. All hydrolysates retained alkaline peptidase activity throughout the process. Alcalase-treated hydrolysates exhibited significantly higher peptidase activity and hydrolysis degree compared to autolysis. At 60 min, Alc-0.24 reached peptidase activity levels similar to Alc-2, and by 30 min, both had comparable degrees of hydrolysis. ABTS·+ scavenging activity increased over time for Alc-0.24, with both Alcalase® 2.4L concentrations outperforming autolysis. No significant differences were found between Alc-0.24 and Alc-2. Although all hydrolysates showed DPPH scavenging activity, no significant differences were detected between treatments or reaction times. These findings highlight the potential for producing value-added protein hydrolysates from Argentine hake waste.
|
| format | Article |
| id | doaj-art-e6cd1eb4553a4ba2b6dff4f9b4f5cdf1 |
| institution | Kabale University |
| issn | 2683-7951 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Instituto Nacional de Investigación y Desarrollo Pesquero (INIDEP) |
| record_format | Article |
| series | Marine and Fishery Sciences |
| spelling | doaj-art-e6cd1eb4553a4ba2b6dff4f9b4f5cdf12025-01-16T02:57:26ZengInstituto Nacional de Investigación y Desarrollo Pesquero (INIDEP)Marine and Fishery Sciences2683-79512025-01-0138210.47193/mafis.3822025010106From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L Clara Liebana0Nair de los Ángeles Pereira1Analia Fernández-Gimenez2Maria Florencia Fangio3Instituto de Investigaciones Marinas y Costeras (IIMyC-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata (UNMdP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), CC 1260, Mar del Plata, ArgentinaInstituto de Investigaciones Marinas y Costeras (IIMyC-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata (UNMdP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), CC 1260, Mar del Plata, ArgentinaInstituto de Investigaciones Marinas y Costeras (IIMyC-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata (UNMdP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), CC 1260, Mar del Plata, ArgentinaDepartamento de Química y Bioquímica, Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata (UNMdP), Funes 3350, B7602AYL - Mar del Plata, Argentina - Instituto de Investigaciones Físicas de Mar del Plata (IFIMAR-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata (UNMdP), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Funes 3350, B7602AYL - Mar del Plata, Argentina The valorization of fishery byproducts is essential to reduce waste and create high-value products. Waste from Argentine hake (Merluccius hubbsi) could enhance its functional and antioxidant properties through hydrolysis, releasing peptides with bioactive properties. Protein hydrolysates of Argentine hake were produced through autolysis (Aut) and enzymatic hydrolysis using Alcalase® 2.4L at concentrations of 0.24% and 2% (v/v) (Alc-0.24 and Alc-2), respectively, over 150 min. Alkaline peptidase activity, degree of hydrolysis, and antioxidant activity were assessed using 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2’-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) radical ABTS·+ scavenging assays. All hydrolysates retained alkaline peptidase activity throughout the process. Alcalase-treated hydrolysates exhibited significantly higher peptidase activity and hydrolysis degree compared to autolysis. At 60 min, Alc-0.24 reached peptidase activity levels similar to Alc-2, and by 30 min, both had comparable degrees of hydrolysis. ABTS·+ scavenging activity increased over time for Alc-0.24, with both Alcalase® 2.4L concentrations outperforming autolysis. No significant differences were found between Alc-0.24 and Alc-2. Although all hydrolysates showed DPPH scavenging activity, no significant differences were detected between treatments or reaction times. These findings highlight the potential for producing value-added protein hydrolysates from Argentine hake waste. https://ojs.inidep.edu.ar/index.php/mafis/article/view/403Waste managementfish protein hydrolysatepeptidase activityhydrolysis degreeantioxidant property |
| spellingShingle | Clara Liebana Nair de los Ángeles Pereira Analia Fernández-Gimenez Maria Florencia Fangio From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L Marine and Fishery Sciences Waste management fish protein hydrolysate peptidase activity hydrolysis degree antioxidant property |
| title | From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L |
| title_full | From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L |
| title_fullStr | From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L |
| title_full_unstemmed | From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L |
| title_short | From waste to value: protein hydrolysates from byproducts of the Argentine hake (Merluccius hubbsi) processing using endogenous enzymes and Alcalase® 2.4L |
| title_sort | from waste to value protein hydrolysates from byproducts of the argentine hake merluccius hubbsi processing using endogenous enzymes and alcalase r 2 4l |
| topic | Waste management fish protein hydrolysate peptidase activity hydrolysis degree antioxidant property |
| url | https://ojs.inidep.edu.ar/index.php/mafis/article/view/403 |
| work_keys_str_mv | AT claraliebana fromwastetovalueproteinhydrolysatesfrombyproductsoftheargentinehakemerlucciushubbsiprocessingusingendogenousenzymesandalcalase24l AT nairdelosangelespereira fromwastetovalueproteinhydrolysatesfrombyproductsoftheargentinehakemerlucciushubbsiprocessingusingendogenousenzymesandalcalase24l AT analiafernandezgimenez fromwastetovalueproteinhydrolysatesfrombyproductsoftheargentinehakemerlucciushubbsiprocessingusingendogenousenzymesandalcalase24l AT mariaflorenciafangio fromwastetovalueproteinhydrolysatesfrombyproductsoftheargentinehakemerlucciushubbsiprocessingusingendogenousenzymesandalcalase24l |