Pumpkin leaf-isolated RuBisCO as a protein source for bioactive peptides
Autori
Mijalković, JelenaŠekuljica, Nataša
Jakovetić Tanasković, Sonja
Luković, Nevena
Pavlović, Neda
Bakrač, Jelena
Knežević-Jugović, Zorica
Konferencijski prilog (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) is a non-allergenic, easily digestible protein found in the leaves of C3 plants, accounting for up to 50% of the total. It is similar to the FAO's ideal protein and is offered as a valuable alternative for meeting nutritional requirements. Plant-based proteins provide amino acids for human cells development and act as precursors of bioactive peptides. Protein sources and proteolytic enzymes are crucial for producing bioactive peptides effectively.
This research aimed to optimize the hydrolysis of pumpkin leaf-isolated protein in terms of time and type of process (one or two-step) using endo- and exo-peptidases. Efficiency was assessed using SDS-PAGE electrophoresis, quantitative hydrolysis analysis, and peptides' capacity to chelate Fe2+ ions and scavenge ABTS•+ radical cations. The peptide molecular weight was determined by implementing the size-exclusion UFLC method.
The highest degree of hydrolysis, which is correlated with... higher antioxidant activity, was shown by Alcalase and Everlase (19.5%), and Neutrase (21.5%) with a tendency to favor Neutrase due to more favorable process conditions and a more sensory-acceptable product. Hydrolysis with Neutrase-Flavourzyme during 225 min yielded hydrolyzates with a 43.5% degree of hydrolysis, and antioxidant activities of 0.74 μmol TEAA/mg (i.e. 48%) and 0.30 μmol EEAA/mg (i.e. 44%). Five peptide fractions were identified as follows: F1 (> 27 kDa), F2 (20-27 kDa), F3 (10-20 kDa), F4 (3-10 kDa), and F5 (< 3 kDa). By establishing a correlation with antioxidant activity, it has been proven that a large proportion of peptide fractions F3, F4, and F5 were accountable for Neutrase-Flavourzyme hydrolyzate's good antioxidant activity. Examined enzymatic approches contributed to generate the antioxidant peptides from pumpkin-leaf proteins with diverse peptide profiles.
Ključne reči:
Plant-based proteins / RuBisCO / Protease / Bioactive peptides / Size-exclusion UFLCIzvor:
Book of abstracts / 26th Congress of SCTM with international participation 20–23 September 2023 Metropol Lake Resort Ohrid, R. Macedonia, 2023, 149-Izdavač:
- Skopje : Society of chemists and technologists of Macedonia
Finansiranje / projekti:
- MultiPromis - Multifunctional leaf protein and assembled nanocarrier structures delivered by enzyme technology (RS-ScienceFundRS-Ideje-7751519)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200135 (Univerzitet u Beogradu, Tehnološko-metalurški fakultet) (RS-MESTD-inst-2020-200135)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200287 (Inovacioni centar Tehnološko-metalurškog fakulteta u Beogradu doo) (RS-MESTD-inst-2020-200287)
Kolekcije
Institucija/grupa
Tehnološko-metalurški fakultetTY - CONF AU - Mijalković, Jelena AU - Šekuljica, Nataša AU - Jakovetić Tanasković, Sonja AU - Luković, Nevena AU - Pavlović, Neda AU - Bakrač, Jelena AU - Knežević-Jugović, Zorica PY - 2023 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6913 AB - RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) is a non-allergenic, easily digestible protein found in the leaves of C3 plants, accounting for up to 50% of the total. It is similar to the FAO's ideal protein and is offered as a valuable alternative for meeting nutritional requirements. Plant-based proteins provide amino acids for human cells development and act as precursors of bioactive peptides. Protein sources and proteolytic enzymes are crucial for producing bioactive peptides effectively. This research aimed to optimize the hydrolysis of pumpkin leaf-isolated protein in terms of time and type of process (one or two-step) using endo- and exo-peptidases. Efficiency was assessed using SDS-PAGE electrophoresis, quantitative hydrolysis analysis, and peptides' capacity to chelate Fe2+ ions and scavenge ABTS•+ radical cations. The peptide molecular weight was determined by implementing the size-exclusion UFLC method. The highest degree of hydrolysis, which is correlated with higher antioxidant activity, was shown by Alcalase and Everlase (19.5%), and Neutrase (21.5%) with a tendency to favor Neutrase due to more favorable process conditions and a more sensory-acceptable product. Hydrolysis with Neutrase-Flavourzyme during 225 min yielded hydrolyzates with a 43.5% degree of hydrolysis, and antioxidant activities of 0.74 μmol TEAA/mg (i.e. 48%) and 0.30 μmol EEAA/mg (i.e. 44%). Five peptide fractions were identified as follows: F1 (> 27 kDa), F2 (20-27 kDa), F3 (10-20 kDa), F4 (3-10 kDa), and F5 (< 3 kDa). By establishing a correlation with antioxidant activity, it has been proven that a large proportion of peptide fractions F3, F4, and F5 were accountable for Neutrase-Flavourzyme hydrolyzate's good antioxidant activity. Examined enzymatic approches contributed to generate the antioxidant peptides from pumpkin-leaf proteins with diverse peptide profiles. PB - Skopje : Society of chemists and technologists of Macedonia C3 - Book of abstracts / 26th Congress of SCTM with international participation 20–23 September 2023 Metropol Lake Resort Ohrid, R. Macedonia T1 - Pumpkin leaf-isolated RuBisCO as a protein source for bioactive peptides SP - 149 UR - https://hdl.handle.net/21.15107/rcub_technorep_6913 ER -
@conference{ author = "Mijalković, Jelena and Šekuljica, Nataša and Jakovetić Tanasković, Sonja and Luković, Nevena and Pavlović, Neda and Bakrač, Jelena and Knežević-Jugović, Zorica", year = "2023", abstract = "RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) is a non-allergenic, easily digestible protein found in the leaves of C3 plants, accounting for up to 50% of the total. It is similar to the FAO's ideal protein and is offered as a valuable alternative for meeting nutritional requirements. Plant-based proteins provide amino acids for human cells development and act as precursors of bioactive peptides. Protein sources and proteolytic enzymes are crucial for producing bioactive peptides effectively. This research aimed to optimize the hydrolysis of pumpkin leaf-isolated protein in terms of time and type of process (one or two-step) using endo- and exo-peptidases. Efficiency was assessed using SDS-PAGE electrophoresis, quantitative hydrolysis analysis, and peptides' capacity to chelate Fe2+ ions and scavenge ABTS•+ radical cations. The peptide molecular weight was determined by implementing the size-exclusion UFLC method. The highest degree of hydrolysis, which is correlated with higher antioxidant activity, was shown by Alcalase and Everlase (19.5%), and Neutrase (21.5%) with a tendency to favor Neutrase due to more favorable process conditions and a more sensory-acceptable product. Hydrolysis with Neutrase-Flavourzyme during 225 min yielded hydrolyzates with a 43.5% degree of hydrolysis, and antioxidant activities of 0.74 μmol TEAA/mg (i.e. 48%) and 0.30 μmol EEAA/mg (i.e. 44%). Five peptide fractions were identified as follows: F1 (> 27 kDa), F2 (20-27 kDa), F3 (10-20 kDa), F4 (3-10 kDa), and F5 (< 3 kDa). By establishing a correlation with antioxidant activity, it has been proven that a large proportion of peptide fractions F3, F4, and F5 were accountable for Neutrase-Flavourzyme hydrolyzate's good antioxidant activity. Examined enzymatic approches contributed to generate the antioxidant peptides from pumpkin-leaf proteins with diverse peptide profiles.", publisher = "Skopje : Society of chemists and technologists of Macedonia", journal = "Book of abstracts / 26th Congress of SCTM with international participation 20–23 September 2023 Metropol Lake Resort Ohrid, R. Macedonia", title = "Pumpkin leaf-isolated RuBisCO as a protein source for bioactive peptides", pages = "149", url = "https://hdl.handle.net/21.15107/rcub_technorep_6913" }
Mijalković, J., Šekuljica, N., Jakovetić Tanasković, S., Luković, N., Pavlović, N., Bakrač, J.,& Knežević-Jugović, Z.. (2023). Pumpkin leaf-isolated RuBisCO as a protein source for bioactive peptides. in Book of abstracts / 26th Congress of SCTM with international participation 20–23 September 2023 Metropol Lake Resort Ohrid, R. Macedonia Skopje : Society of chemists and technologists of Macedonia., 149. https://hdl.handle.net/21.15107/rcub_technorep_6913
Mijalković J, Šekuljica N, Jakovetić Tanasković S, Luković N, Pavlović N, Bakrač J, Knežević-Jugović Z. Pumpkin leaf-isolated RuBisCO as a protein source for bioactive peptides. in Book of abstracts / 26th Congress of SCTM with international participation 20–23 September 2023 Metropol Lake Resort Ohrid, R. Macedonia. 2023;:149. https://hdl.handle.net/21.15107/rcub_technorep_6913 .
Mijalković, Jelena, Šekuljica, Nataša, Jakovetić Tanasković, Sonja, Luković, Nevena, Pavlović, Neda, Bakrač, Jelena, Knežević-Jugović, Zorica, "Pumpkin leaf-isolated RuBisCO as a protein source for bioactive peptides" in Book of abstracts / 26th Congress of SCTM with international participation 20–23 September 2023 Metropol Lake Resort Ohrid, R. Macedonia (2023):149, https://hdl.handle.net/21.15107/rcub_technorep_6913 .