Next Article in Journal
Synthesis of Uracil-Iodonium(III) Salts for Practical Utilization as Nucleobase Synthetic Modules
Next Article in Special Issue
Determination of N-Carbamylglutamate in Feeds and Animal Products by High Performance Liquid Chromatography Tandem Mass Spectrometry
Previous Article in Journal
The Synthesis of New Thermal Stable Schiff Base/Ester Liquid Crystals: A Computational, Mesomorphic, and Optical Study
Previous Article in Special Issue
Green Extraction of Phenolic Acids from Artemisia argyi Leaves by Tailor-Made Ternary Deep Eutectic Solvents
Open AccessArticle

Sequence Identification of Bioactive Peptides from Amaranth Seed Proteins (Amaranthus hypochondriacus spp.)

1
Chemistry Investigation Center, Universidad Autónoma del Estado de Hidalgo, Carretera Pachuca-Tulancingo km 4.5, Mineral de la Reforma Hidalgo C.P. 46067, Mexico
2
Biotechnology Department, Universidad Autónoma Metropolitana, Unidad Iztapalapa, Mexico City C.P. 55355, Mexico
3
Universidad de Santiago de Compostela, Campus Lugo, 15705 Santiago de Compostela, 27002 A Coruña, Spain
*
Author to whom correspondence should be addressed.
Molecules 2019, 24(17), 3033; https://doi.org/10.3390/molecules24173033
Received: 1 June 2019 / Revised: 1 August 2019 / Accepted: 3 August 2019 / Published: 21 August 2019
(This article belongs to the Special Issue Analytical Technology in Nutrition Analysis)
Amaranthus hypochondriacus spp. is a commonly grown cereal in Latin America, known for its high protein content. The objective of this study was to separate and identify bioactive peptides found in amaranth seeds through enzymatically-assisted hydrolysis using alcalase and flavourzyme. Hydrolysis was carried out for each enzyme separately and compared to two-step continuous process where both enzymes were combined. The biological activity of the resulting three hydrolysates was analyzed, finding, in general, higher bioactive potential of the hydrolysate obtained in a continuous process (combined enzymes). Its fractions were separated by RP-HPLC, and their bioactivity was analyzed. In particular, two fractions showed the highest biological activity as ACE inhibitors with IC50 at 0.158 and 0.134, thrombin inhibitors with IC50 of 167 and 155, and antioxidants in ABTS assay with SC50 at 1.375 and 0.992 mg/L, respectively. Further sequence analysis of the bioactive peptides was carried out using MALDI-TOF, which identified amino acid chains that have not been reported as bioactive so far. Bibliographic survey allowed identification of similarities between peptides reported in amaranth and other proteins. In conclusion, amaranth proteins are a potential source of peptides with multifunctional activity. View Full-Text
Keywords: amaranth protein; flavourzyme; alcalase; bioactive peptides; hydrolysates amaranth protein; flavourzyme; alcalase; bioactive peptides; hydrolysates
Show Figures

Figure 1

MDPI and ACS Style

Ayala-Niño, A.; Rodríguez-Serrano, G.M.; González-Olivares, L.G.; Contreras-López, E.; Regal-López, P.; Cepeda-Saez, A. Sequence Identification of Bioactive Peptides from Amaranth Seed Proteins (Amaranthus hypochondriacus spp.). Molecules 2019, 24, 3033.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop