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The aim of this experimental study is to investigate the inhibitive properties of polyglycol and polyglycol+KCl aqueous solutions on hydrate formation, which causes serious fluid flow problems, especially during deepwater drilling operations. As the petroleum industry continues to search oil in deeper and deeper seas, the possibility of facing hydrate problems during drilling operations increases because of the suitable conditions for hydrate formation. The main goal of this study is to investigate the hydrate inhibition capacity (thermodynamic and/or kinetic inhibition) of polyglycol and KCl which are mainly used in drilling fluids for shale inhibition and wellbore stability. A high pressure hydrate forming reactor is used to form and dissociate methane hydrate from aqueous solutions of polyglycol and polyglycol+KCl. In total 10 experiments were carried out, 5 of them with 0%, 1%, 3%, 5% and 7 % by volume of polyglycol solutions (Group-A experiments). The remaining 5 experiments (Group-B) had 8% by weight of KCl in solution in addition to the same polyglycol concentrations of Group-A experiments. Among the two chemicals tested for their hydrate inhibiting potentials, polyglycol did not exhibit any thermodynamic inhibition capacity while KCl was observed to have the ability of hydrate inhibition thermodynamically. On the other hand, increase in polyglycol concentration at constant KCl concentration (Group-B) increases the hydrate formation depression capacity of KCl. Polyglycol inhibits methane hydrate formation kinetically. The higher the polyglycol concentration in aqueous solution, the lower is the initial rate of methane hydrate formation (corresponding to first 15 minutes of hydrate formation). On the other hand, there exists a slower change of methane hydrate formation rate as polyglycol concentration increases.

Orientador: Glaucia Maria Pastore / Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos / Made available in DSpace on 2018-08-07T18:42:38Z (GMT). No. of bitstreams: 1 Pace_LuizWanderleyBratfisch_D.pdf: 1299912 bytes, checksum: 1fd286322b5f78c4d7eae6e8c0a42f42 (MD5) Previous issue date: 2006 / Resumo: A síntese de ésteres utilizando biocatalisadores está se tornando técnica e economicamente viável, devido aos benefícios apresentados pelo uso destes catalisadores, aos constantes investimentos no desenvolvimento de enzimas com maior rendimento, estabilidade e atividade enzimática e ao surgimento de enzimas imobilizadas que possibilitam o reuso várias vezes. Considerando o grande potencial das enzimas como biocatalisadores e apesar de já existerem no mercado algumas aplicações definidas, existe necessidade de estudo e aprimoramento dos processos enzimáticos nesta área, principalmente para estabelecer os processos em escala industrial. Neste trabalho foi estudada a síntese de quatro ésteres de poliglicóis, com propriedade surfactante e antiespumante, utilizando lipases e esterases como biocatalisadores. Foram avaliadas nove enzimas comerciais de diferentes fornecedores e selecionado três; as quais se apresentaram mais adequadas para os ésteres a serem obtidos e nas condições de processo que possibilitem a produção dos mesmos em escala industrial. A seleção das enzimas e condições reacionais foram baseadas nos resultados obtidos das 227 reações realizadas em laboratório e 2 reações em escala piloto. Três ésteres foram obtidos com sucesso por biocatálise, sendo dois com propriedades de surfactante e um com propriedades de antiespumante, igual ou superior aos produtos obtidos por processo químico. Todos os produtos obtidos por biocatálise apresentaram coloração mais clara, indicando menor oxidação, quando comparados com os produtos obtidos pelo processo químico, no qual é utilizado catalisador ácido e altas temperaturas. Nos estudos realizados foi possível comprovar a seletividade da esterase avaliada como biocatalisador, ao alterar um dos componentes do substrato. As esterificações foram realizadas em diferentes temperaturas, concentrações de enzimas e tempos de reação, visando obter condições de processo que permitam a produção dos ésteres em escala industrial. O acompanhamento das reações foi realizado através de análise titulométrica e espectrometria no infravermelho. A identidade dos ésteres obtidos por biocatálise frente aos ésteres obtidos por processo químico, foi realizada através das técnicas de espectrometria no infravermelho, cromatografia em camada delgada e cromatografia líquida de alta eficiência. A faixa de temperatura ideal para a obtenção dos ésteres estudados foi de 70 ¿ 75º C, com tempo de reação entre 8 e 10 horas e porcentagem de esterificação de até 95%. Os resultados obtidos comprovam que lipases e esterases podem ser utilizadas, na síntese de ésteres de poliglicóis, em substituição aos catalisadores utilizados nos processos químicos, permitindo a redução da temperatura e pressão do processo. Com isso, aumenta a segurança do processo e reduz os impactos ambientais, pela redução do consumo de energia e uso de catalisadores menos agressivos ao meio ambiente. Salientamos que as enzimas são produzidas com insumos renováveis e processos que causam mínimos impactos ao meio ambiente / Abstract: The ester biocatalyst synthesis is becoming technical and economically viable, based on the associated benefits by the use of these catalyst, the constant investiments in enzymes development with high yield, stability, enzymatic activity and new immobilized enzymes that allow multiple uses of the same material. Considering the great potential of enzymes as biocatalysts and although there is already in the market some defined applications, there is still the need to study and improve the enzymatic processes in this area, mainly to establish processes on industrial scale. In this paper, the synthesis of four polyglycol esters with defoamer and surfactant properties, using lipases and esterases as biocalyst, were studied. Nine commercial enzymes coming from different suppliers were evaluated and three were selected; which showed to be more adequate for the esters to be obtained and for the conditions of the process to allow their use on industrial scale. The selection of enzymes and the reacting conditions were based on the results obtained from the 227 reactions runned in the laboratory and 2 reactions in pilot scale. Three esters were successfully obtained by biocatalysis, two with surfactant properties and one with defoamer properties, with the same or better performance than the products obtained by the chemical process. All products obtained by biocatalyst process presented light color, indicating less oxidation, when compared with products obtained by chemical process, where an acid catalyst and high temperatures are used. Esterase biocatalyst selectivity was demonstrated when one component of the substrate was changed. Esterification was carried out in different temperatures, enzymes concentrations, and reaction times, in order to obtain adequate process conditions that allowed the production of esters on industrial scale. Reaction tracking was done using titration analysis and infrared spectrometry. The identity of esters obtained by biocatalysis in relation to esters obtained by chemical process was established through infrared spectrometry techniques, thin layer chromatography, and high performance liquid chromatography. The ideal temperature range to obtain the esters studied was 70 ¿ 75º C, with a reaction time between 8 to 10 hours and esterification percentage up to 95%. The results obtained prove that lipases and esterases can be used in the synthesis of polyglycol esters in substitution to catalysts used in chemical processes, allowing temperature and pressure reduction in the process. Thus, the process safety increases and environmental impacts are reduced, by the reduction of energy consumption and the use of less aggressive catalyst to the environment. It is important to point out that the enzymes are produced with renewable materials and processes that cause minimum impact to the environment / Doutorado / Doutor em Ciência de Alimentos