Ciencias Exactas y Ciencias de la Salud

Permanent URI for this collectionhttps://hdl.handle.net/11285/551014

Pertenecen a esta colección Tesis y Trabajos de grado de los Doctorados correspondientes a las Escuelas de Ingeniería y Ciencias así como a Medicina y Ciencias de la Salud.

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  • Tesis de doctorado
    Evaluation of solid-state fermentation of edible insects (S. purpurascens and T. molitor) with Aspergillus Oryzae and its potential use in bread and gluten-free bread
    (Instituto Tecnológico y de Estudios Superiores de Monterrey, 2025-05-20) Pérez Rodríguez, Elizabeth; Ibarra Herrera, Celeste Concepción; emipsanchez; Molina Rosell, Cristina; Cortés Ferré, Héctor Emmanuel; Calderón Oliver, Mariel; Escuela de Ingeniería y Ciencias; Campus Monterrey; Pérez Carrillo, Esther
    Interest in incorporating edible insects into the diet is increasing due to their nutritional content. The most critical challenges are related to the low acceptability of the consumer due to changes in taste, color, and textural properties of the final product when edible insect flour is added. This work proposes the study and use of solid-state fermentation (SSF) of edible insects to improve its incorporation in food products. Tenebrio molitor (yellow mealworm) and Sphenarium purpurascens (grasshopper “chapulín” in Spanish) were suggested as study objects of SSF with Aspergillus oryzae. Fermented and unfermented insect powder was chemically and techno-functionally characterized. The effect of the incorporation of fermented and unfermented insects’ powder in wheat bread (with yellow mealworm and chapulín), maize and rice bread (with chapulín) were evaluated on different stages. Rheological characterization of dough and physical, chemical, textural, nutritional, and sensory analysis of bread was used to compare the effect of fermentation. Incorporating grasshopper powder into gluten-free and wheat bread significantly increased protein, ash, fat, and total dietary fiber content. Fermentation significantly increased protein and dietary fiber and produce changes on techno- functional properties on T. molitor and S. purpurascens powders. Techno-functional changes were reflected on dough rheology and then on wheat bread texture decreasing hardness as positive result. In both, wheat and gluten-free bread (maize and rice), rheological analysis revealed that fermented grasshopper flour reduced setback viscosity, an important factor in bread quality as it is linked to starch retrogradation and shelf-life stability. This reduction in setback suggests that fermentation may improve the freshness of bread. This study indicates that fermentation modifies insect powder which impacts on bread quality, potentially due to changes in protein, enzymes interactions, and techno-functional properties. The findings suggest that fermentation provides greater benefits for Sphenarium purpurascens than for Tenebrio molitor. Moreover, fermented grasshopper powder shows improved performance in terms of dough rheology and bread texture in wheat-based formulations compared to gluten-free ones. Additionally, the data support the potential of S. purpurascens as an ingredient capable of significantly enhancing the nutritional value of bread. These results align with recent research emphasizing the nutritional advantages of edible insects as protein-rich food sources.
  • Tesis de doctorado
    Development of novel polymer-protein conjugates and characterization of chromatographic supports
    (Instituto Tecnológico y de Estudios Superiores de Monterrey, 2021-06-10) Sánchez Trasviña, Calef; SANCHEZ TRASVIÑA, CALEF; 655893; Rito Palomares, Marco Antonio; emipsanchez; Aguilar Jiménez, Oscar Alejandro; Zavala Arcos, Judith; Chuck Hernández, Cristina Elizabeth; School of Engineering and Sciences; Campus Monterrey; Mayolo Deloisa, Karla Patricia
    Protein versatility has positioned them as a high-value biotechnological product. Among protein applications, its use as a therapeutic agent is highlighted. However, some therapeutic proteins need a modification process to increase their pharmacokinetic properties. During the protein modification process, the purification step, mainly performed by chromatography, represents a critical stage in ensuring the safety of modified therapeutics proteins. Being chromatography the main purification method, it is mandatory to fully understand the effect of all its operational variables on the separation performance. This work presents a deep analysis of chromatographic strategies used to purify modified therapeutic proteins commercially available. Furthermore, an alternative protein modification process is presented using N-(2-hydroxypropyl) methacrylamide (HPMA) polymer and its purification by chromatography. Besides, the development and characterization of PEGylated monoliths as an alternative to purify PEGylated proteins is performed. Finally, the characterization of core-shell particles being used as chromatographic support is developed. The results showed that the selection of purification strategies of commercial modified proteins depends on physicochemical properties of both protein and attached molecule and is highly dependent on the matrix where the protein is recovered. HPMA copolymers can be conjugated with Ribonuclease A (RNase A) under non-demanding conditions (PO4-3 buffer 50 mM pH 5.1 + 20 mM NaBH3CN). The new conjugates showed higher hydrophobic behavior than the native protein being this feature exploited by hydrophobic interaction chromatography (using 1.5 M (NH4)2SO4) to separate the conjugates from the unreacted protein. On the other hand, PEGylated monoliths can separate PEGylated RNase A and even isoforms when large polyethylene glycol molecules (>20 kDa) are attached to the monolith. Lastly, the CaptoTM Core 700 resin structural (50.4 nm pore size, 4.18 µm shell thickness, and 90.7 µm particle size) and adsorptive properties allowed modeling and adsorption prediction of two model proteins. In combination, all these results represent new knowledge in the polymer-protein technology and chromatography areas that proportionate guidelines to purify a wide range of molecules such as native, recombinant, and modified proteins efficiently.
En caso de no especificar algo distinto, estos materiales son compartidos bajo los siguientes términos: Atribución-No comercial-No derivadas CC BY-NC-ND http://www.creativecommons.mx/#licencias
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