Ciencias Exactas y Ciencias de la Salud

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Evaluation of the bioactive properties of peptides obtained from the enzymatic hydrolysis of mesquite (Prosopis laevigata) cotyledon flour proteins
(Instituto Tecnológico y de Estudios Superiores de Monterrey, 2024) Sanchez Jimenez, Omar; Mata Gomez, Marco Arnulfo; Ramirez Jimenez, Aurea Karina; Cervantes Avilés, Pabel Antonio; Escuela de Ingeniería y Ciencias; Campus Monterrey; Luna Vital, Diego Armando
For several decades, Mexico has faced a series of health problems that reduce the quality of life of its inhabitants. Diseases such as diabetes, hypertension, respiratory infections, and cancer are responsible for the primary mortality rates in the country and require immediate attention. Fortunately, Mexico also has privileged plant biodiversity, with a cultural meaning firmly rooted in Mexican society reflected in its traditions, customs, gastronomy, and increasingly frequent in the research of molecules with bioactive properties. In this sense, it is especially relevant to study those species with inherent value to the communities where they are endemic but that have remained outside of scientific scrutiny as potential sources of molecules that help solve current health challenges. The species Prosopis laevigata, commonly known as mesquite, is a clear example of a plant with economic, medicinal, and nutritional importance, but that has been little studied, which is why it represents an area of opportunity in contributing to the literature. Bioactive peptides have been positioned as attractive study molecules due to a series of properties, including potent biological activity, relative safety compared to other small molecules, diversity of target molecules, and ease of production. The objective of this work was to evaluate the bioactive peptides derived from the enzymatic hydrolysis of the proteins present in the seed of Prosopis laevigata in order to determine their antioxidant potential, as well as their antimicrobial, cytotoxic, and enzymatic inhibitory capacity. The peptides presented SC50 values of 81 and 89 µg/mL for the fractions smaller and larger than 5 kDa, respectively, demonstrating strong antioxidant capacity in the ABTS assay. Similarly, a reducing power of 0.250 and 0.156 was obtained in the FRAP test, reaching similar conclusions. The cell viability assay against the HepG2 cell line showed a cytotoxic effect at high concentrations of the peptides (8 mg/mL). On the other hand, the antimicrobial assay demonstrated an inhibition in the growth of S. aureus but was inefficient in inhibiting the growth of E. coli, suggesting a selective inhibition mechanism. Finally, it was demonstrated that the peptides have the ability to inhibit the activity of α-amylase. In addition, it was evident that the type of inhibition depends on the fraction used as an inhibitor, resulting in a competitive type of inhibition for those peptides with a size less than 5 kDa and mixed for peptides greater than 5 kDa. Altogether, the results revealed the great potential of P. laevigata peptides as bioactive molecules and justified the importance of continuing to study them to implement them in a functional product in response to the prevention or treatment of health challenges in Mexico.
Study of black bean (Phaseolus vulgaris) and quinoa (Chenopodium quinoa) flours as a source of peptides and their effect on DPP-IV inhibition
(Instituto Tecnológico y de Estudios Superiores de Monterrey, 2023) Jacobo Téllez, Diana Laura; Chuck Hernández, Cristina Elizabeth; mtyahinojosa, emipsanchez; Escalante Aburto, Anayansi; Rodríguez Sifuentes, Lucio; School of Engineering and Sciences; Campus Monterrey; Soria Hernández, Cintya Geovanna
Plant-based proteins can be beneficial for the environment and health purposes. Nowadays, diet and a sedentary lifestyle are the cause of several health problems, such as obesity, cardiovascular diseases, cancer, and diabetes. Black beans and quinoa are important sources of plant-based proteins due to their high protein content and well-balanced amino acid presence. Black beans and quinoa are considered nutritious and rich in bioactive peptides (BP), characterized by their positive impact on healthy body functions. BP's antidiabetic, antimicrobial, antioxidant, and antihypertensive properties are some health benefits. This work aimed to evaluate black bean flour with two types of process (extruded and non-extruded) and two varieties of quinoa (white and black) as a source of bioactive peptides with potential DPP-IV inhibitory activity. All flours were evaluated at two levels of milling. The study of the raw materials encompassed a particle size analysis, a morphological analysis using a scanning electron microscope (SEM) and a proximate characterization. Black bean with level 1 milling had 98% of particles with a smaller diameter than 813.25±8.35 m, while for black bean flour with level 2 milling, this diameter was 566.54±43.82 m, showing that the second milling yielded flour with finer particles. On the other side, white quinoa with level 1 milling had 98% of particles with a maximum diameter of 697.21±110.40 m, while white quinoa with level 2 milling had 98% of particles with a maximum diameter of 546.28±26.33 m. The morphological and proximate analysis showed that samples were rich in starch and protein. The quinoa flour varieties had 15.13±1.55 and 15.51±0.70% of protein (white and black quinoa flour, respectively), the black bean flour had 18.93±1.63%, and the extruded black bean flour had 22.75±0.44% of protein. All flour samples had between 62.26±1.46% to 63.45±1.55% of total carbohydrates. Afterward, the protein fraction was extracted by alkaline procedure at pH 12, resulting in high extraction yield and purity. Black bean with finer milling had the highest protein extraction yield with 82.87±3.97%, and fine-milled white quinoa had the highest protein purity with 61.33±2.83%. Protein hydrolysis was then carried out using 1% alcalase (% w/w of protein) for 0,1, 2, 4 and 6 hours at 60 °C. The degree of hydrolysis (DH) was determined, with extruded black bean showing the highest DH (354.8%). The electrophoretic profile showed the different protein fractions (globulin, albumin and phaseolin). It is also noticeable that the bands are much broader below 10 kDa, showing that the molecular weight is lower, which could mean that the hydrolysis process successfully reduced the protein length. DPP-IV inhibitory activity was determined, and the results showed that white quinoa and black bean hydrolysates have the highest relative inhibition, with 50.00%. The inhibitory activity of DPP-IV contributes to the potential use of hydrolysates obtained from quinoa and black bean as an ingredient with nutraceutical functions. DPP-IV inhibition is a preventive and therapeutic mechanism of action for type 2 diabetes.

Ciencias Exactas y Ciencias de la Salud

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