TY - JOUR
T1 - Protein hydrolysates from salmon heads and cape hake by-products
T2 - comparing enzymatic method with subcritical water extraction on bioactivity properties
AU - Pires, Carla
AU - Leitão, Matilde
AU - Sapatinha, Maria
AU - Gonçalves, Amparo
AU - Oliveira, Helena
AU - Nunes, Maria Leonor
AU - Teixeira, Bárbara
AU - Mendes, Rogério
AU - Camacho, Carolina
AU - Machado, Manuela
AU - Pintado, Manuela
AU - Ribeiro, Ana Rita
AU - Vieira, Elsa F.
AU - Delerue-Matos, Cristina
AU - Lourenço, Helena Maria
AU - Marques, António
N1 - Publisher Copyright:
© 2024 by the authors.
PY - 2024/7/30
Y1 - 2024/7/30
N2 - Fish by-products can be converted into high-value-added products like fish protein hydrolysates (FPHs), which have high nutritional value and are rich in bioactive peptides with health benefits. This study aims to characterise FPHs derived from salmon heads (HPSs) and Cape hake trimmings (HPHs) using Alcalase for enzymatic hydrolysis and Subcritical Water Hydrolysis (SWH) as an alternative method. All hydrolysates demonstrated high protein content (70.4–88.7%), with the degree of hydrolysis (DH) ranging from 10.7 to 36.4%. The peptide profile of FPHs indicated the breakdown of proteins into small peptides. HPSs showed higher levels of glycine and proline, while HPHs had higher concentrations of glutamic acid, leucine, threonine, and phenylalanine. Similar elemental profiles were observed in both HPHs and HPSs, and the levels of Cd, Pb, and Hg were well below the legislated limits. Hydrolysates do not have a negative effect on cell metabolism and contribute to cell growth. HPSs and HPHs exhibited high 2,2′–azino-bis(3 ethylbenzthiazoline-6)-sulfonic acid (ABTS) radical scavenging activity, Cu2+ and Fe2+ chelating activities, and angiotensin-converting enzyme (ACE) inhibitory activity, with HPHs generally displaying higher activities. The α-amylase inhibition of both FPHs was relatively low. These results indicate that HPHs are a promising natural source of nutritional compounds and bioactive peptides, making them potential candidates for use as an ingredient in new food products or nutraceuticals. SWH at 250 °C is a viable alternative to enzymatic methods for producing FPHs from salmon heads with high antioxidant and chelating properties.
AB - Fish by-products can be converted into high-value-added products like fish protein hydrolysates (FPHs), which have high nutritional value and are rich in bioactive peptides with health benefits. This study aims to characterise FPHs derived from salmon heads (HPSs) and Cape hake trimmings (HPHs) using Alcalase for enzymatic hydrolysis and Subcritical Water Hydrolysis (SWH) as an alternative method. All hydrolysates demonstrated high protein content (70.4–88.7%), with the degree of hydrolysis (DH) ranging from 10.7 to 36.4%. The peptide profile of FPHs indicated the breakdown of proteins into small peptides. HPSs showed higher levels of glycine and proline, while HPHs had higher concentrations of glutamic acid, leucine, threonine, and phenylalanine. Similar elemental profiles were observed in both HPHs and HPSs, and the levels of Cd, Pb, and Hg were well below the legislated limits. Hydrolysates do not have a negative effect on cell metabolism and contribute to cell growth. HPSs and HPHs exhibited high 2,2′–azino-bis(3 ethylbenzthiazoline-6)-sulfonic acid (ABTS) radical scavenging activity, Cu2+ and Fe2+ chelating activities, and angiotensin-converting enzyme (ACE) inhibitory activity, with HPHs generally displaying higher activities. The α-amylase inhibition of both FPHs was relatively low. These results indicate that HPHs are a promising natural source of nutritional compounds and bioactive peptides, making them potential candidates for use as an ingredient in new food products or nutraceuticals. SWH at 250 °C is a viable alternative to enzymatic methods for producing FPHs from salmon heads with high antioxidant and chelating properties.
KW - FPH
KW - Fish waste
KW - Enzymatic hydrolysis
KW - SWH
KW - Biochemical composition
KW - Contaminants
KW - Cytotoxicity
KW - Antioxidant
KW - ACE
KW - α-amylase inhibitory activities
UR - http://www.scopus.com/inward/record.url?scp=85200759318&partnerID=8YFLogxK
U2 - 10.3390/foods13152418
DO - 10.3390/foods13152418
M3 - Article
C2 - 39123610
SN - 2304-8158
VL - 13
JO - Foods
JF - Foods
IS - 15
M1 - 2418
ER -