TY - JOUR
T1 - Impact of thermal treatment and hydrolysis by alcalase and cynara cardunculus enzymes on the functional and nutritional value of okara
AU - Voss, Glenise B.
AU - Osorio, Hugo
AU - Valente, Luísa M. P.
AU - Pintado, Manuela E.
N1 - Funding Information:
Author G. B. Voss gratefully acknowledges CAPES/ Brazil Federal Agency - for the research fellowship administered for funding this work. This work was supported by National Funds from FCT - Fundação para a Ciência e a Tecnologia through project UID/Multi/50016/2013 and project BiValBi - Biotechnologies to Valorize the regional Biodiversity in Latin America (Refª PIRSES-GA-2013-611493 BI_1). The MALDI-TOF/TOF approach was performed at the Proteomics i3S Scientific Platform with the assistance of Hugo Osorio.
Funding Information:
Author G. B. Voss gratefully acknowledges CAPES/ Brazil Federal Agency - for the research fellowship administered for funding this work. This work was supported by National Funds from FCT - Funda??o para a Ci?ncia e a Tecnologia through project UID/Multi/50016/2013 and project BiValBi - Biotechnologies to Valorize the regional Biodiversity in Latin America (Ref? PIRSES-GA-2013-611493 BI_1). The MALDI-TOF/TOF approach was performed at the Proteomics i3S Scientific Platform with the assistance of Hugo Osorio.
Publisher Copyright:
© 2019
PY - 2019/8
Y1 - 2019/8
N2 - Enzymatic hydrolysis of dried okara (autoclaved and non-autoclaved) with Alcalase (AL) and Cynara cardunculus extract (CY) was studied, assessing the impact of heat treatment and hydrolysis on potential antioxidant and antihypertensive activities of final hydrolysates. This study showed that the thermal treatment (sterilization at 121 °C, 1 atm and 15 min) facilitated the enzymatic access to substrate and increased the degree of hydrolysis (DH), especially for AL (37.9%) when compared to CY (3.6%). The antioxidant activity of dried Okara (either autoclaved or not) when hydrolysed with AL was higher (4.2 mg Trolox/mL) than that observed for CY. Additionally, the potential ACE-inhibitory activity was high for samples hydrolysed with both enzymes, however the highest ACE inhibition was also found for AL (IC50 = 9.97 μg/mL). This study allowed the identification of new peptide sequences in dried okara hydrolysed with both enzymes, and some sequences that can explain their bioactivities. The results indicate that dried okara hydrolysates can either be used as functional ingredient or as food supplement for blood pressure lowering or antioxidant applications in the future.
AB - Enzymatic hydrolysis of dried okara (autoclaved and non-autoclaved) with Alcalase (AL) and Cynara cardunculus extract (CY) was studied, assessing the impact of heat treatment and hydrolysis on potential antioxidant and antihypertensive activities of final hydrolysates. This study showed that the thermal treatment (sterilization at 121 °C, 1 atm and 15 min) facilitated the enzymatic access to substrate and increased the degree of hydrolysis (DH), especially for AL (37.9%) when compared to CY (3.6%). The antioxidant activity of dried Okara (either autoclaved or not) when hydrolysed with AL was higher (4.2 mg Trolox/mL) than that observed for CY. Additionally, the potential ACE-inhibitory activity was high for samples hydrolysed with both enzymes, however the highest ACE inhibition was also found for AL (IC50 = 9.97 μg/mL). This study allowed the identification of new peptide sequences in dried okara hydrolysed with both enzymes, and some sequences that can explain their bioactivities. The results indicate that dried okara hydrolysates can either be used as functional ingredient or as food supplement for blood pressure lowering or antioxidant applications in the future.
KW - Antihypertensive activity
KW - Antioxidant activity
KW - Bioactivity
KW - Enzymatic hydrolysis
KW - Okara
KW - Peptide
UR - http://www.scopus.com/inward/record.url?scp=85066080848&partnerID=8YFLogxK
U2 - 10.1016/j.procbio.2019.05.010
DO - 10.1016/j.procbio.2019.05.010
M3 - Article
AN - SCOPUS:85066080848
SN - 1359-5113
VL - 83
SP - 137
EP - 147
JO - Process Biochemistry
JF - Process Biochemistry
ER -