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      Optimization of Sorghum Kafirin Extraction Conditions and Identification of Potential Bioactive Peptides

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          Abstract

          The interest in extracting kafirins (KAF), the main storage protein from sorghum grain has recently increased due to its gluten-free content and the significant scientific evidence showing the health benefits of the bioactive peptides from cereal grains in human diets. The objectives were to obtain the highest percentage of KAF extraction using amyloglucosidase as pretreatment to increase the extraction yield and predict the bioactive peptides in the KAF. In this study, pretreatments with amyloglucosidase increased the extraction yield of KAF compared with extraction methods using only ethanol and sodium metabisulfite. Two protein fragment sequences were identified from KAF extract and were evaluated for potential bioactive peptide using the BIOPEP-UWM database, which suggest that KAF proteins from white sorghum may be considered as good precursors of dipeptidyl peptidase-inhibitor, angiotensin-converting enzyme inhibitor, antioxidant and hypotensive peptides following chymotrypsin, thermolysin, and subtilisin and their combination. Average scores aligned using PeptideRanker confirmed KAF proteins' potential sources of bioactive peptides with over 5 peptides scored over 0.8. In addition, 31 unexplored peptide sequences that could have biological activity were identified. Our results suggest that KAF can be used in the peptide productions with potential biological activity and beyond.

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          Novel food and non-food uses for sorghum and millets

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            Advancement and prospects of bioinformatics analysis for studying bioactive peptides from food-derived protein: Sequence, structure, and functions

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              Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: Hydrolysis kinetic, purification and molecular docking study.

              In this study, sweet sorghum grain protein (SSGP) was hydrolyzed using alcalase yielding ACE inhibitory peptides. A kinetic model was proposed to describe the enzymolysis process of SSGP. The kinetic parameters, a and b, were determined according to experimental data. It was found that the model was reliable to describe the kinetic behaviour for SSGP hydrolysis by alcalase. After hydrolysis, the SSGP hydrolysate with DH of 19% exhibited the strongest ACE inhibitory activity and the hydrolysate was then used to isolate ACE inhibitory peptides. A novel ACE inhibitory peptide was successfully purified from this hydrolysate by ultrafiltration, ion exchange chromatography, gel filtration chromatography, and reversed-phased high performance liquid chromatography (RP-HPLC). The amino acid sequence of the purified peptide was identified as Thr-Leu-Ser (IC50=102.1 μM). The molecular docking studies revealed that the ACE inhibition of the tripeptide was mainly attributed to its C-terminal Ser, which can effectively interact with the S1 and S2 pockets of ACE. Our studies suggest that the tripeptide from the SSGP hydrolysate can be utilized to develop functional food ingredients or pharmaceuticals for prevention of hypertension.
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                Author and article information

                Journal
                Biores Open Access
                Biores Open Access
                biores
                BioResearch Open Access
                Mary Ann Liebert, Inc., publishers (140 Huguenot Street, 3rd FloorNew Rochelle, NY 10801USA )
                2164-7844
                2164-7860
                September 2020
                2020
                September 2020
                : 9
                : 1
                : 198-208
                Affiliations
                [ 1 ]Instituto Tecnológico de Tepic. Av. Tecnológico No. 2595, Col. Lagos del Country, Tepic, Nayarit, México.
                [ 2 ]Catedra CONACyT, Facultad de Enfermería y Nutrición, Universidad Autónoma de San Luis Potosí, Av. Niño Artillero No. 130, Zona Universitaria, S.L.P., México.
                [ 3 ]Catedra CONACyT, Facultad de Ingeniería, Universidad Autónoma de Querétaro, Carretera Chichimequillas s/n, El Marqués, Querétaro, México.
                Author notes
                [*] [ * ]Address correspondence to: Luz E. Alcántara-Quintana, PhD, Catedra CONACyT, Facultad de Enfermería y Nutrición, Universidad Autónoma de San Luis Potosí, Av. Niño Artillero No. 130, Zona Universitaria, San Luis Potosi 78240, México luz.alcantara@ 123456uaslp.mx
                Article
                10.1089/biores.2020.0013
                10.1089/biores.2020.0013
                7484892
                32923174
                970dcc8a-4291-4723-aa78-90cad3bce2d3
                © Tania P. Castro-Jácome et al., 2020; Published by Mary Ann Liebert, Inc.

                This Open Access article is distributed under the terms of the Creative Commons License ( http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : Accepted August 11, 2020
                Page count
                Figures: 2, Tables: 6, References: 45, Pages: 11
                Categories
                Original Research Article

                white sorghum,kafirins,amyloglucosidase,bioactive peptides

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