Características bromatológicas y concentración de aflatoxina B1 en granos de Theobroma cacao. Nueva Cajamarca. Julio 2017 - Febrero 2018

El presente trabajo de investigación tuvo como objetivo determinar las carácterísticas bromatológicas y la concentración de aflatoxina B1 en granos de Theobroma cacao, procedente de la ciudad de Nueva cajamarca desde julio del 2017 hasta febrero del 2018. Fueron recolectados 87 muestras de granos de cacao, de tres almacenes diferentes, con 27 muestras cada una. El análisis se llevó a cabo en el laboratorio de Cincias Biológicas de la Universidad Nacional Pedro Ruiz Gallo, teniendo en cuenta los métodos señalados por las Normas Técnicas Peruanas, Asociación Peruana Productores de Cacao, Federación de Comercio de Cacao (FCC), y Asociacion Oficial de Químicos Analíticos (AOAC); en lo que respecta a la cuantificación de la AFB1 se utilizó el método de inmunoensayo enzimático competitivo directo (ELISA). Para caracteristicas bromatológicas, se obtuvieron valores normales, las caracteristicas físicas cualitativas fueron 93.10% para olor, 97.70% color, 96.5% tamaño y 98.55% forma. Las caracteristicas físicas cuantitativas presentaron valores normales, el 69.98/100g para recuento, 142.46g para peso de 100 granos teniendo relación proporcional con 1.42g del peso de un grano. Se encontró una presencia razonable de residuos y/o defectos; el 0.4%, 0,5%, 0.4% para materia extraña; 0.7%, 0.5%, 0.6% para granos planos; 0.6%, 0,6%, 0.5% para granos múltiples; y 0.7%, 0.5%, 0.5% para granos rotos. Los defectos encontrados durante la prueba de corte; el 0.374% para granos enmohecidos, 0.998% para granos pizarrosos, 3.482% para granos violaceos, 0.786% para granos germinados y 0.55% para granos atacado por insectos. Las características sensoriales presentó atributos más resaltantes alcanzando una intensidad media; amargo 87.4%, astrigencia 90.8%, acidez 72.4%, cacao 93.1%, floral 64.4%. El porcentaje promedio de las caracteristicas fisico-quimicas fueron normales para humedad 6.46%, extracto seco 93.54%, proteínas 16.27%, grasas 44.24%, fibra bruta 3.48%, cenizas 3.46%. La cuantificación de Aflatoxina B1, determinó que las 87 muestras analizadas; el 21.84% (19 muestras) presentó contaminación, con una concentración promedio de 6.46 ppb y una concentración máxima de 33.14 ppb y de las muestras positivas el 26.32% sobrepasó el límite máximo permisible de 8 ppb, el cacao procedente del almacén N° 01 presentó mayor cantidad de muestras positivas 44.83%. Los porcentajes y promedios obtenidos para las características bromatológicas y AFB1 en granos de cacao del presente trabajo de investigación, demostraron que el cacao procedente de los tres centros de acopio y/o almacenes presentaron características de calidad propia de la zona

Mapeo de la inversión privada en Lambayeque al 2014

En los últimos años la economía en el interior del país está generando una innegable fuerza motora que contribuye en el crecimiento económico, generando fuentes de empleo, eslabonamientos productivos y desarrollando nuevas capacidades económicas. En esa realidad juega un rol muy importante la iniciativa privada. Reconociendo la importancia del sector privado en este contexto se hace necesario que el sector público realice un acercamiento para que los esfuerzos sean complementarios y los resultados más alentadores desde el punto de vista económico y social. En esa óptica es imperativo el conocimiento del real esfuerzo de los inversionistas privados, sus montos de inversión, los espacios territoriales, las tendencias, los perfiles y su percepción del clima de inversiones que se ofrece en la región. Sin embargo esta información es muy dispersa y en muchos casos hasta reservada por los inversionistas. En la primera parte del estudio se analiza la dinámica sectorial en base a los indicadores de desempeño de la producción regional y la percepción de analistas financieros sobre la dinámica del sector privado, con el objeto de priorizar los sectores. En los siguientes capítulos se analiza a cada sector cuantificando las inversiones más importantes, los espacios territoriales de las inversiones, las tendencias de cada sector y finalmente se analiza en forma sucinta el clima de inversiones en la región.In recent years the economy inside the country is creating an undeniable driving force that contributes to economic growth, generating employment opportunities, production linkages and developing new economic capabilities. In that reality plays a very important role the private sector. Recognizing the importance of the private sector in this context it is necessary for the public sector to make an approach for that efforts are complementary and the encouraging results from an economic and social perspective. In this perspective it is imperative that knowledge of the real effort of private investors, their investment amounts, territorial spaces, trends, profiles, and their perception of the investment climate in the region is provided. However, this information is scattered and often booked up by investors. In the first part of the study the sectoral dynamics based on the performance indicators of regional production and perception of financial analysts on the dynamics of the private sector, in order to prioritize the sectors analyzed. In the following chapters each sector is analyzed by quantifying the most important investments, territorial spaces investments, trends in each sector and finally succinctly analyzes the investment climate in the regionInstituto de Economía y Empresa (Lambayeque, Perú

Functional and structural studies of the regulators of Type IV Pilus biogenesis in Xanthomonas citri subsp. citri

O pilus tipo IV (T4P) são finos e flexíveis filamentos encontrados na superfície de uma ampla gama de bactérias Gram-negativas, Gram-positivas e archaea. O T4P desempenha um rol crucial no estilo de vida bacteriano ao estar envolvido em uma variedade de funções incluindo motilidade, aderência, formação de biofilme, patogenicidade, transformação natural e na infecção por fagos. Várias das proteínas requeridas para a biossíntese e regulação do T4P se estendem através do periplasma conectado a membrana interna e externa. O T4P são estruturas dinâmicas que sofrem ciclos de extensão e retração energizados por duas ATPases associadas com a membrana interna bacteriana. Durante a extensão, PilB, a ATPase de biossíntese do T4P, estimula a polimerização do pilus a partir de monômeros de pilinas localizados na membrana interna, através de um mecanismo ainda desconhecido. Duas proteínas, FimX e PilZ estão envolvidas na regulação da biossíntese do T4P via interações com PilB e nocautes de esses genes acabam com a biogênese e função do T4P. Neste trabalho, nós determinamos a estrutura cristalográfica do complexo binário formado pelo domínio N-terminal de PilB (PilBNt, resíduos 12-163) e a PilZ com uma resolução de 1.7 Å. As interações entre PilB e PilZ envolve uma superfície hidrofóbica formada por aminoácidos altamente conservados na família não canônica de domínios PilZ. Mutações ou deleções de alguns destes resíduos em PilZ enfraquecem a interação PilB-PilZ e afeta a função do T4P. Nós também observamos que esta interação induz mudanças conformacionais no domínio PilBNt, revelando a possibilidade de um rearranjo estrutural funcionalmente relevante da região Nterminal de PilB permitindo a sua interação com PilM, conectando a ATPase PilB como a maquinaria do T4P. Nós mostramos que PilB, PilZ e FimX podem formar um complexo ternário estável com uma massa molar aparente de ~600 kDa, sugerindo uma estequiometria de 6PilB:6PilZ:2FimX. Também observamos que FimX incrementa a atividade ATPase do complexo PilB-PilZ. O c-di-GMP e o ATPγS (um análogo não hidrolisável do ATP) induz mudanças conformacionais em FimX e no complexo PilB-PilZ, respectivamente, e estabiliza o complexo ternário PilB-PilZ-FimX. Além disso, PilB, PilZ e FimX localizam em um dos polos da célula (polo líder) em células de X. citri e a localização polar dirige a orientação da motilidade twitching. Finalmente, o T4P é necessário para a exitosa infecção de X. citri pelo fago ΦXacm4-11. Nossos resultados sugerem que asinterações entre PilB-PilZ-FimX estariam envolvidas na regulação da função de PilB, onde sinais especificas sentidas pelos domínios de FimX seriam transmitidas por PilZ até PilB.Bacterial type IV pili (T4P) are thin and flexible filaments found on the surface of a wide range of Gram-negative bacteria and play a crucial role in their lifestyles due to their involvement in a variety of functions including motility, adherence, biofilm formation, pathogenicity, natural transformation and phage infection. Several proteins required for the biogenesis and regulation of T4P span the periplasm connecting both the inner and outer membranes. T4P are dynamic structures that undergo cycles of extension and retraction powered by two hexameric ATPases associated with the bacterial inner membrane. During extensions, the T4P assembly ATPase PilB stimulates the polymerization of pilin monomers from the inner membrane, though the precise mechanism is unknown. Two proteins, FimX and PilZ are involved in the regulation of T4P biogenesis via interactions with the PilB and knockouts of these proteins abolish T4P biogenesis. Here, we determined the crystal structure of the binary complex made up of the PilB N-terminal domain (PilBNt, residues 12- 163) bound to PilZ at 1.7Å resolution. PilZ interactions with PilB involve a hydrophobic surface made up of amino acids conserved in a non-canonical family of PilZ domains. Mutations or deletion of some these amino acids in PilZ weaken the PilZ-PilB interaction and affect T4P function. This interaction induces significant conformational changes in the PilBNt domain, suggesting that structural rearrangements of the PilB N-terminal domains could be important for its interaction with PilM, connecting the ATPase PilB with T4P machinery. We show also that full-length PilB, PilZ and FimX can form a stable ternary complex with apparent molecular weight of ~600 kDa, suggestive of a 6PilB:6PilZ:2FimX stoichiometry and that FimX increases the ATPase activity of the PilB PilZ complex. C-diGMP and ATPγS (non-hydrolysable analog of ATP) induce conformational changes in FimX and in PilB-PilZ, respectively, and stabilize the ternary PilB-PilZ-FimX complex. In addition, we show that PilB, PilZ and FimX localize at one cell pole (leading pole) that drives the movement in X. citri. Finally, the T4P is necessary for successful infection of X. citri cells by phage ΦXacm4-11. Our results suggest how FimXPilZPilB interactions could be involved in the regulation of PilB function, where specific environmental signals sensed by FimX domains could be transmitted via PilZ to PilB

Functional and structural studies of the regulators of Type IV Pilus biogenesis in Xanthomonas citri subsp. citri

O pilus tipo IV (T4P) são finos e flexíveis filamentos encontrados na superfície de uma ampla gama de bactérias Gram-negativas, Gram-positivas e archaea. O T4P desempenha um rol crucial no estilo de vida bacteriano ao estar envolvido em uma variedade de funções incluindo motilidade, aderência, formação de biofilme, patogenicidade, transformação natural e na infecção por fagos. Várias das proteínas requeridas para a biossíntese e regulação do T4P se estendem através do periplasma conectado a membrana interna e externa. O T4P são estruturas dinâmicas que sofrem ciclos de extensão e retração energizados por duas ATPases associadas com a membrana interna bacteriana. Durante a extensão, PilB, a ATPase de biossíntese do T4P, estimula a polimerização do pilus a partir de monômeros de pilinas localizados na membrana interna, através de um mecanismo ainda desconhecido. Duas proteínas, FimX e PilZ estão envolvidas na regulação da biossíntese do T4P via interações com PilB e nocautes de esses genes acabam com a biogênese e função do T4P. Neste trabalho, nós determinamos a estrutura cristalográfica do complexo binário formado pelo domínio N-terminal de PilB (PilBNt, resíduos 12-163) e a PilZ com uma resolução de 1.7 Å. As interações entre PilB e PilZ envolve uma superfície hidrofóbica formada por aminoácidos altamente conservados na família não canônica de domínios PilZ. Mutações ou deleções de alguns destes resíduos em PilZ enfraquecem a interação PilB-PilZ e afeta a função do T4P. Nós também observamos que esta interação induz mudanças conformacionais no domínio PilBNt, revelando a possibilidade de um rearranjo estrutural funcionalmente relevante da região Nterminal de PilB permitindo a sua interação com PilM, conectando a ATPase PilB como a maquinaria do T4P. Nós mostramos que PilB, PilZ e FimX podem formar um complexo ternário estável com uma massa molar aparente de ~600 kDa, sugerindo uma estequiometria de 6PilB:6PilZ:2FimX. Também observamos que FimX incrementa a atividade ATPase do complexo PilB-PilZ. O c-di-GMP e o ATPγS (um análogo não hidrolisável do ATP) induz mudanças conformacionais em FimX e no complexo PilB-PilZ, respectivamente, e estabiliza o complexo ternário PilB-PilZ-FimX. Além disso, PilB, PilZ e FimX localizam em um dos polos da célula (polo líder) em células de X. citri e a localização polar dirige a orientação da motilidade twitching. Finalmente, o T4P é necessário para a exitosa infecção de X. citri pelo fago ΦXacm4-11. Nossos resultados sugerem que asinterações entre PilB-PilZ-FimX estariam envolvidas na regulação da função de PilB, onde sinais especificas sentidas pelos domínios de FimX seriam transmitidas por PilZ até PilB.Bacterial type IV pili (T4P) are thin and flexible filaments found on the surface of a wide range of Gram-negative bacteria and play a crucial role in their lifestyles due to their involvement in a variety of functions including motility, adherence, biofilm formation, pathogenicity, natural transformation and phage infection. Several proteins required for the biogenesis and regulation of T4P span the periplasm connecting both the inner and outer membranes. T4P are dynamic structures that undergo cycles of extension and retraction powered by two hexameric ATPases associated with the bacterial inner membrane. During extensions, the T4P assembly ATPase PilB stimulates the polymerization of pilin monomers from the inner membrane, though the precise mechanism is unknown. Two proteins, FimX and PilZ are involved in the regulation of T4P biogenesis via interactions with the PilB and knockouts of these proteins abolish T4P biogenesis. Here, we determined the crystal structure of the binary complex made up of the PilB N-terminal domain (PilBNt, residues 12- 163) bound to PilZ at 1.7Å resolution. PilZ interactions with PilB involve a hydrophobic surface made up of amino acids conserved in a non-canonical family of PilZ domains. Mutations or deletion of some these amino acids in PilZ weaken the PilZ-PilB interaction and affect T4P function. This interaction induces significant conformational changes in the PilBNt domain, suggesting that structural rearrangements of the PilB N-terminal domains could be important for its interaction with PilM, connecting the ATPase PilB with T4P machinery. We show also that full-length PilB, PilZ and FimX can form a stable ternary complex with apparent molecular weight of ~600 kDa, suggestive of a 6PilB:6PilZ:2FimX stoichiometry and that FimX increases the ATPase activity of the PilB PilZ complex. C-diGMP and ATPγS (non-hydrolysable analog of ATP) induce conformational changes in FimX and in PilB-PilZ, respectively, and stabilize the ternary PilB-PilZ-FimX complex. In addition, we show that PilB, PilZ and FimX localize at one cell pole (leading pole) that drives the movement in X. citri. Finally, the T4P is necessary for successful infection of X. citri cells by phage ΦXacm4-11. Our results suggest how FimXPilZPilB interactions could be involved in the regulation of PilB function, where specific environmental signals sensed by FimX domains could be transmitted via PilZ to PilB

The Xanthomonas type IV pilus

Type IV pili, a special class of bacterial surface filaments, are key behavioral mediators for many important human pathogens. However, we know very little about the role of these structures in the lifestyles of plant-associated bacteria. Over the past few years, several groups studying the extensive genus of Xanthomonas spp. have gained insights into the roles of played by type IV pili in bacteria-host interactions and pathogenesis, motility, biofilm formation, and interactions with bacteriophages. Protein-protein interaction studies have identified T4P regulators and these, along with structural studies, have begun to reveal some of the possible molecular mechanisms that may control the extension/retraction cycles of these dynamic filaments.Fil: Dunger, Ricardo German. Universidade de Sao Paulo; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ciencias Agrarias; ArgentinaFil: Llontop, Edgar. Universidade de Sao Paulo; BrasilFil: Guzzo, Cristiane R.. Universidade de Sao Paulo; BrasilFil: Farah, Chuck S.. Universidade de Sao Paulo; Brasi

Business consulting a la empresa Smart Reasons S.R.L.

La presente investigación tiene como objetivo principal analizar a Smart Reasons, una empresa dedicada a la implementación de soluciones tecnológicas que ofrece diferentes alternativas en el área de desarrollo de software. Se identificaron cuatro problemas en la organización luego de aplicar el método empírico-analítico y la descomposición de los elementos para estudiar sus causas y realizar un análisis profundo del contenido de las entrevistas semi estructuradas efectuadas vía telefónica al Gerente General, Gerente Comercial, Gerente de Desarrollo I + D de la empresa, además de las reuniones con el Gerente General para discutir dichos problemas que están afectando el pleno desarrollo de sus actividades y los resultados económicos esperados. El problema principal que se determinó tras la realización del business consulting fue la disminución de las ventas en el 2018, debido a que los ingresos percibidos no generaron ningún tipo de oportunidad de crecimiento para la compañía. La problemática fue originada por la falta de respaldo económico, la ausencia de un mapa estratégico, la falta de un área de administración de contratos (área legal interna) y la pérdida de negocio del rubro minero porque los ingresos de la organización se basaban en un 100% de las ventas en dicho sector. Por esa razón, se diseñó un mapa estratégico para darle solución al problema de la disminución de las ventas, lograr tanto excelencia operativa como liderazgo en producto y finalmente la consolidación de las relaciones con los clientes. La implementación de este mapa estratégico requiere de una inversión total de S/ 55,000.00; dicho monto será recuperado en un período de 2.27 años, con un beneficio / costo de 2.09. Esto significa que por cada sol que los socios de la empresa inviertan en el mapa estratégico, recuperan 1.09 soles, convirtiéndolo en un proyecto económicamente viable.The main objective of this research is to analyze Smart Reasons, a company dedicated to the implementation of technological solutions that offers different alternatives in the software development area. Four problems in the organization were identified after applying the empirical-analytical method and the decomposition of the elements to study their causes and carry out a deep analysis of the content of the semi-structured interviews carried out by telephone with the General Manager, Commercial Manager, R&D Development Manager of the company, in addition to the meetings with the General Manager to discuss the problems that are affecting the full development of their activities and the expected economic results. The main problem determined after the business consulting was the decrease in sales in 2018, since the income received did not offer any kind of growth opportunity. The problem was originated by the lack of financial support, the absence of strategic plan, the lack of contract management area (internal legal area) and the loss of the mining business because the organization´s income was based on 100% of sales in that sector. For this reason, a strategic map was designed to solve the problem of sales decline, achieve both operational excellence and product leadership, and finally the consolidation of customer relationships. The implementation of this strategic map requires a total investment of S/55,000; this amount will be recovered in a period of 2.27 years, with a benefit/cost of 2.09. This means that for every Sol that the partners of the company invest in the plan, they will recover S/1.09, making it an economically viable project.Tesi

Bactericidal type IV secretion system homeostasis in Xanthomonas citri

Several Xanthomonas species have a type IV secretion system (T4SS) that injects a cocktail of antibacterial proteins into neighbouring Gram-negative bacteria, often leading to rapid lysis upon cell contact. This capability represents an obvious fitness benefit since it can eliminate competition while the liberated contents of the lysed bacteria could provide an increase in the local availability of nutrients. However, the production of this Mega Dalton-sized molecular machine, with over a hundred subunits, also imposes a significant metabolic cost. Here we show that the chromosomal virB operon, which encodes the structural genes of this T4SS in X. citri, is regulated by the conserved global regulator CsrA. Relieving CsrA repression from the virB operon produced a greater number of T4SSs in the cell envelope and an increased efficiency in contact-dependent lysis of target cells. However, this was also accompanied by a physiological cost leading to reduced fitness when in co-culture with wild-type X. citri. We show that T4SS production is constitutive despite being downregulated by CsrA. Cells subjected to a wide range of rich and poor growth conditions maintain a constant density of T4SSs in the cell envelope and concomitant interbacterial competitiveness. These results show that CsrA provides a constant though partial repression on the virB operon, independent of the tested growth conditions, in this way controlling T4SS-related costs while at the same time maintaining X. citri’s aggressive posture when confronted by competitor

Importance of the β5−β6 Loop for the structure, catalytic efficiency and stability of carbapenem-hydrolyzing class D β-Lactamase subfamily OXA-143

The class D beta-lactamase OXA-143 has been described as an efficient penicillinase, oxacillinase, and carbapenemase. The D224A variant, known as OXA-231, was described in 2012 as exhibiting less activity toward imipenem and increased oxacillinase activity. Additionally, the P227S mutation was reported as a case of convergent evolution for homologous enzymes. To investigate the impact of both mutations (D224A and P227S), we describe in this paper a deep investigation of the enzymatic activities of these three homologues. OXA-143(P227S) presented enhanced catalytic activity against ampicillin, oxacillins, aztreonam, and carbapenems. In addition, OXA-143(P227S) was the only member capable of hydrolyzing ceftazidime. These enhanced activities were due to a combination of a higher affinity (lower K-m) and a higher turnover number (higher k(cat)). We also determined the crystal structure of apo OXA-231. As expected, the structure of this variant is very similar to the published OXA-143 structure, except for the two M223 conformations and the absence of electron density for three solvent-exposed loop segments. Molecular dynamics calculations showed that both mutants experience higher flexibility compared to that of the wild-type form. Therefore, our results illustrate that D224A and P227S act as deleterious and positive mutations, respectively, within the evolutionary path of the OXA-143 subfamily toward a more efficient carbapenemase583436043616CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQCOORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE MINAS GERAIS - FAPEMIGFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESP438316/2018-5não temAPQ:90941142011/0777-5; 2017/17303-7; 2017/22822-3The authors thank the facilities NMR Laboratory, Chemistry Institute IQ-UNICAMP, Núcleo de Computação Científica da Universidade do Estado de São Paulo (NCC/GridUNESP), and Centro Nacional de Processamento de Alto Desempenho em São Paulo (CENAPAD-SP) for computational resources, The authors also thank the Chemistry Institute of the University of Campinas and the Chemistry Institute of the University of São Paulo. Ronaldo Nagem and Tiago Brandão are acknowledged for their financial support during time spent at UFMG. The authors finally thank Stefanya Velázques Gómez for helpful discussions, Cláudio F. Tormena and Carlos Ramos for kindly helping with reagents and equipment, and Annelize Z. B. Aragão for support with mutations and protein purificatio

Antibacterial T6SS effectors with a VRR-Nuc domain are structure-specific nucleases

The type VI secretion system (T6SS) secretes antibacterial effectors into target competitors. Salmonella spp. encode five phylogenetically distinct T6SSs. Here, we characterize the function of the SPI-22 T6SS of Salmonella bongori showing that it has antibacterial activity and identify a group of antibacterial T6SS effectors (TseV1–4) containing an N-terminal PAAR-like domain and a C-terminal VRR-Nuc domain encoded next to cognate immunity proteins with a DUF3396 domain (TsiV1–4). TseV2 and TseV3 are toxic when expressed in Escherichia coli and bacterial competition assays confirm that TseV2 and TseV3 are secreted by the SPI-22 T6SS. Phylogenetic analysis reveals that TseV1–4 are evolutionarily related to enzymes involved in DNA repair. TseV3 recognizes specific DNA structures and preferentially cleave splayed arms, generating DNA double-strand breaks and inducing the SOS response in target cells. The crystal structure of the TseV3:TsiV3 complex reveals that the immunity protein likely blocks the effector interaction with the DNA substrate. These results expand our knowledge on the function of Salmonella pathogenicity islands, the evolution of toxins used in biological conflicts, and the endogenous mechanisms regulating the activity of these toxins

Proyecto de Investigación Aplicada 1 - IN45 - 202102

Descripción: El curso Proyecto de Investigación Aplicada 1 es un curso de verificación en el que el estudiante desarrolla un proyecto de Ingeniería Industrial bajo las condiciones, recursos y limitaciones de un trabajo real. El proyecto se concluye en el curso de Proyecto de Investigación Aplicada 2. El curso comprende la identificación de un 1problema a resolver, el soporte teórico correspondiente, el análisis y diagnóstico de la situación o problema, y el diseño y desarrollo de las propuestas de mejora. A lo largo del desarrollo del proyecto, el estudiante demuestra el adecuado uso de criterios de ciencias e ingeniería, así como de técnicas y herramientas de la Ingeniería Industrial. Los proyectos se desarrollan principalmente bajo las modalidades de proyectos de mejora o investigación, correspondiendo en todos los casos al diseño o rediseño de procesos o sistemas de producción de bienes y servicios, proporcionando una solución o propuesta dentro del ámbito de la Ingeniería Industrial. Propósito: El curso Proyecto de Investigación Aplicada 1 permite al estudiante desarrollar un proyecto de Ingeniería Industrial aplicando los conceptos, técnicas y herramientas aprendidos a lo largo de la carrera, bajo condiciones, recursos y limitaciones de un trabajo real. El curso contribuye directamente al desarrollo de las competencias generales Comunicación Oral, Comunicación Escrita y Pensamiento Crítico, todas a nivel 3 y a las competencias específicas de ABET: (2) Tiene la capacidad de aplicar el diseño de ingeniería para producir soluciones que satisfagan las necesidades especificas con consideraciones de salud publica seguridad y bienestar, así como factores globales, culturales, sociales, ambientales y económicos. (nivel 3) (6) Tiene la capacidad de desarrollar y llevar a cabo una experimentación adecuada, analizar e interpretar datos, y usar el juicio de ingeniería para sacar conclusiones. (nivel 3) (7) Tiene la capacidad de adquirir y aplicar nuevos conocimientos según sea necesario, utilizando estrategias de aprendizaje apropiadas. (nivel 3) Los requisitos del curso son: IN216 Gerencia de Proyectos, IN97 Logística Integrada y Cadena de Abastecimientos e IN397 Seminario de Investigación Académica II (Ing)