Ever since the Meiji Restoration, Japanese political leaders, under a strong impact from the West, had urged the complete abolition of feudalism. By the turn of the century, they had consolidated their political power by means of putting the Emperor system on a firm footing, and had introduced and considerably developed a modern capitalist economy. Opposed to these radical changes were the socialist and right-wing movements, but for different reasons. The socialists, whose theories were based entirely on European ideas, opposed the authoritarianism of the Meiji government, and in international politics supported pacifism. The rightwing movements criticised the government for its pursuit of extreme Europeanisation, and for its bourgeois and liberal ethos. They also encouraged Japanese territorial expansion into Asian countries. Because the socialist movements were suppressed by the government, the rightwing ones gradually came to hold the initiative among Japanese social movements. Kita Ikki was a radical opponent of the authoritarian form of government, but was also a vigorous advocate of Japanese imperialism as a means of overcoming Western imperialism. These two positions, usually held by two antagonistic sectors of Japanese society, were logically linked in Kita's thought on the basis of his belief in social evolution and the class struggle. He criticised the theory of the national polity for its misrepresentation of Japanese history and social change. For him, the Meiji Restoration had accomplished a legal revolution, which led to the establishment of a kōmin kokka (public state), in which both the Emperor and the people owed their rights and duties to the state. He believed that an economic revolution alone would suffice to bring about social democracy in Japan, a revolution which could be carried out peacefully by means of the ballot. Total class war was unnecessary. But contrary to pacifist socialists, Kita encouraged the international class struggle as the only means of abolishing the "age of imperialism." Evolution in the international world had not yet reached a point whereby a World Federation could peacefully settle conflicts among nations. By 1919, however, Kita had become an advocate of a coup d'état in order to overthrow the corrupt government, and, by means of the Emperor's prerogatives, to hasten economic change at home as well as pursue a revolutionary policy abroad. The central theme in this study is the logical link between Kita's critique of the national polity and his advocacy of war. Because of the latter, as well as his support of a coup d'état, Kita has been labelled the "ideological father of Japanese fascism." Post-war Japanese scholars have concentrated on these "negative" aspects of his thought, and neglected the "positive" ones, namely, his critique of the national polity. Some criticise him for alleged conversion from a socialist to a fascist. This study avoids the fascist label and argues against the notion of changes in his fundamental ideas. Kita's actual writings, especially the recently published ones, reveal that throughout his life he adhered to the basic ideas of social evolution and class struggle. Both remained the foundation of his critique of the national polity as well as his advocacy of war. Kita was never an orthodox socialist, even in his early years, nor a fascist of any kind, even in his later years. His support of a coup d'état was a tactical change made in the light of his critique of the national polity and advocacy of war, and was meant to speed up developments at home and abroad. In the light of post-war democratic development in Japan, Kita's critique of the national polity should be evaluated "positively." The general failure to do so has been due to his advocacy of war and a coup d'état. But if the two strands of thought are logically dependant on the same premises, one cannot have one without the other. The only way to accept Kita's critique of the national polity and at the same time criticise his advocacy of war, is by recognizing that Japan is no longer in the position of a semi-colonised country, and that even though colonised countries may justifiably revolt, they are not thereby entitled to become colonisers themselves. If this is recognised, the recent ideological alliance between Kita and the new left cannot be regarded as harbouring a danger of a fascist revival. / Arts, Faculty of / Political Science, Department of / Graduate

This thesis seeks to study in depth the contribution to Sufism made by the little-known 4th/10th century figure Abū Ṭālib al-Makkī. The first chapter deals with an analysis of the life and works of al-Makkī against the background of the religious milieu of his time. A major section of the thesis (the second and third chapters) provides for the first time in English a translation of the Kitāb al-tawba of al-Makkī. The fourth chapter assesses the originality of al-Makkī's Kitāb al-tawba and compares it with similar Ṣūfī works of the period. The fifth chapter attempts to compare and contrast al-Makkī and al-Ghazālī's approach to Sufism through an analysis of their respective Kitāb al-tawba. It has long been known that in his work on Sufism, al-Ghazālī depended very heavily upon al-Makkī. This thesis conclusively proves this dependence whilst pointing to the more sophisticated presentation of al-Ghazālī. Al-Makkī is shown to have been one of the early Ṣūfī figures who tried to harmonise the views of the Baṣran and Baghdād Ṣūfī groups and to effect a synthesis between moderate Sufism and the Sharī'a.

Tesis para optar al grado de Magíster en Historia mención Historia Europea

Kita Morio has been one of the most successful humorists of Japan's postwar period, but his work has received little attention from scholars. The intent of this study is to provide an introduction to the humorous essays of Kita Morio. In particular, after the principles of the humor mechanism are established, the nature of the essays as a type of I-novel is examined. The focus is then turned to the authorial persona that Kita uses in his humorous essays, and an overview of that manufactured fictional character and the world he inhabits is created. Finally, five individual essays are examined in the context created by the preceding chapters, with particular attention given to the manner in which humor functions in the essays, as well as the manner in which the reader can find comfort in them. Translations of the five essays examined in the final chapter are provided in the Appendix.

As endo-1,4-?-xilanases (EC 3.2.1.8) formam o maior grupo de enzimas hidrolíticas envolvido na degradação da xilana, visto que catalisam a hidrólise aleatória de ligações glicosídicas do tipo ?-1,4 no interior da sua cadeia principal, produzindo xilooligossacarídeos de diferentes tamanhos. Na natureza, essas enzimas estão intimamente relacionadas ao fornecimento de energia para o desenvolvimento dos organismos que as produzem. Em geral, as xilanases são isoladas preferencialmente de bactérias e fungos, e têm demonstrado grande potencial na produção de pães, ração animal, alimentos, bebidas, xilitol e bioetanol. O presente trabalho propôs o isolamento de uma nova endo-1,4-?-xilanase por meio de técnicas de produção e purificação acessíveis que pudessem viabilizar economicamente a integração desse biocatalisador aos processos industriais. O fungo Aspergillus tamarii Kita, oriundo de uma amostra de solo da Mata Atlântica, mostrou-se um bom produtor de xilanases em meio de cultura Adams suplementado com bagaço de cevada, um subproduto das indústrias cervejeiras. Após a otimização do processo de fermentação submersa, o extrato enzimático exibiu duas xilanases em gel de atividade para proteínas nativas, identificadas por espectrometria de massas como glicosil hidrolases pertencentes às famílias 10 e 11. A sacarificação enzimática de três resíduos agroindustriais, com base em um delineamento experimental de misturas, demonstrou que a combinação ternária desses componentes, em iguais proporções, possui considerável relevância para a produção de açúcares fermentáveis, tais como glicose e xilose. Em ensaios de imobilização, a xilanase GH11 foi satisfatoriamente estabilizada em matrizes de caráter iônico e covalente. A imobilização por ligação covalente multipontual em glioxil-agarose elevou a temperatura ótima de atividade de 60 para 65 °C e ofertou um considerável ganho de termoestabilidade ao derivado, que apresentou meia vida de 60 minutos a 80 °C. Além disso, a estabilização da enzima nesse suporte permitiu a produção dos seguintes xilooligossacarídeos: xilobiose, xilotriose, xilotetraose e xilopentaose. A purificação da xilanase GH11 foi realizada por meio de uma única etapa cromatográfica de troca catiônica, com rendimento final de 36,72% e um fator de purificação de 7,43 vezes. A massa molecular da enzima foi estimada em 19,5 kDa. Ademais, a sua estrutura tridimensional foi predita por modelagem comparativa, exibindo como modelo final uma arquitetura do tipo ?-jelly roll, comum às xilanases da família 11. Em ensaios de caracterização, a xilanase apresentou melhor atividade em pH 5,5 e manteve atividade residual superior a 80% na faixa de pH compreendida entre 4,0 e 9,0, durante 24 horas. Em relação à temperatura, a sua atividade ótima foi observada a 60 °C, contudo, a sua termoestabilidade foi mais expressiva a 50 °C, retendo cerca de 70% da sua atividade inicial por 480 minutos. Para a xilana beechwood, os valores de velocidade máxima e constante de dissociação aparente foram iguais a 1.330,20 µmol/min/mg e 8,13 mg/mL, respectivamente. Na concentração de 5 mM, os metais pesados Co2+, Hg+, Pb2+ e Zn2+ apresentaram um ponderável efeito de inibição sobre a xilanase GH11, enquanto que os íons Ba2+ e Ni2+, assim como os compostos ?-mercaptoetanol e DTT, exibiram um aumento superior a 20% em sua atividade. Por fim, a análise em tempo real da atividade xilanásica revelou que o substrato xilopentaose corresponde ao menor xilooligossacarídeo capaz de ser eficientemente hidrolisado. Sendo assim, a nova endo-xilanase GH11 isolada do fungo A. tamarii Kita exibe uma série de propriedades físico-químicas favoráveis a sua aplicabilidade em escala industrial. / The endo-1,4-?-xylanases (EC 3.2.1.8) form the largest group of hydrolytic enzymes involved in the degradation of xylan, since they catalyze the random hydrolysis of ?-1,4 glycosidic bonds within the main chain of this polysaccharide, producing xylooligosaccharides of different sizes. In nature, these enzymes are closely related to supplying energy for the development of the organisms that produce them. In general, xylanases are preferentially isolated from bacteria and fungi, which show great potential in industries as brewing, animal feed, food, beverage, xylitol and bioethanol. The present work proposed the isolation of a new endo-1,4-?-xylanase by available techniques of production and purification that can economically make feasible the integration of this biocatalyst to industrial processes. The fungus Aspergillus tamarii Kita, obtained from a soil sample of the Atlantic Forest, showed to be a good xylanase producer in Adams culture medium supplemented with barley bagasse, a byproduct of breweries. After the optimization of the submerged fermentation process, the crude enzymatic extract exhibited two xylanases in activity gel for native proteins, identified by mass spectrometry as glycosyl hydrolases belonging to families 10 and 11. The enzymatic saccharification of three agroindustrial residues, based on an experimental mixture design, showed that the ternary combination of these components, in equal proportions, has considerable relevance for the production of fermentable sugars, such as glucose and xylose. The xylanase GH11 was satisfactorily stabilized on matrices of ionic and covalent character in immobilization assays. Covalent multipoint immobilization on glyoxyl agarose raised its optimum temperature of activity from 60 to 65 °C and offered a considerable gain in thermostability to the derivative, which presented a half-life of 60 minutes at 80 °C. In addition, enzyme stabilization on this support allowed the production of the following xylooligosaccharides: xylobiose, xylotriose, xylotetraose and xylopentaose. Xylanase GH11 purification was carried out by means of a single cation exchange chromatographic step, with final yield of 36.72% and purification factor of 7.43 times. The molecular mass of this xylanase was estimated as 19.5 kDa. Moreover, its three-dimensional structure was predicted by comparative modeling, exhibiting a ?-jelly roll type folding as a final model, common to xylanases of family 11. In characterization tests, xylanase presented better activity at pH 5.5 and was considerably stable in the pH range of 4.0 to 9.0. Regarding temperature, its optimum activity was observed at 60 °C, however, its thermostability was more expressive at 50 °C, retaining about 70% of its initial activity for 480 minutes. In the presence of beechwood xylan, the values of maximum velocity and the constant of apparent dissociation were 1,330.20 µmol/min/mg and 8.13 mg/mL, respectively. At concentrations of 5 mM, the heavy metals Co2+, Hg+, Pb2+ and Zn2+showed an inhibition effect on the xylanase, whereas Ba2+ and Ni2+ ions, as well as ?-mercaptoethanol and DTT, exhibited an increase of more than 20% in their activity. Finally, the real-time analysis of xylanase activity revealed that the xylopentose substrate corresponds to the lowest xylooligosaccharide capable of being hydrolyzed. Thus, the new endo-xylanase GH11 isolated from the fungus A. tamarii Kita exhibits a series of physicochemical properties favorable to its applicability on an industrial scale.

As endo-1,4-?-xilanases (EC 3.2.1.8) formam o maior grupo de enzimas hidrolíticas envolvido na degradação da xilana, visto que catalisam a hidrólise aleatória de ligações glicosídicas do tipo ?-1,4 no interior da sua cadeia principal, produzindo xilooligossacarídeos de diferentes tamanhos. Na natureza, essas enzimas estão intimamente relacionadas ao fornecimento de energia para o desenvolvimento dos organismos que as produzem. Em geral, as xilanases são isoladas preferencialmente de bactérias e fungos, e têm demonstrado grande potencial na produção de pães, ração animal, alimentos, bebidas, xilitol e bioetanol. O presente trabalho propôs o isolamento de uma nova endo-1,4-?-xilanase por meio de técnicas de produção e purificação acessíveis que pudessem viabilizar economicamente a integração desse biocatalisador aos processos industriais. O fungo Aspergillus tamarii Kita, oriundo de uma amostra de solo da Mata Atlântica, mostrou-se um bom produtor de xilanases em meio de cultura Adams suplementado com bagaço de cevada, um subproduto das indústrias cervejeiras. Após a otimização do processo de fermentação submersa, o extrato enzimático exibiu duas xilanases em gel de atividade para proteínas nativas, identificadas por espectrometria de massas como glicosil hidrolases pertencentes às famílias 10 e 11. A sacarificação enzimática de três resíduos agroindustriais, com base em um delineamento experimental de misturas, demonstrou que a combinação ternária desses componentes, em iguais proporções, possui considerável relevância para a produção de açúcares fermentáveis, tais como glicose e xilose. Em ensaios de imobilização, a xilanase GH11 foi satisfatoriamente estabilizada em matrizes de caráter iônico e covalente. A imobilização por ligação covalente multipontual em glioxil-agarose elevou a temperatura ótima de atividade de 60 para 65 °C e ofertou um considerável ganho de termoestabilidade ao derivado, que apresentou meia vida de 60 minutos a 80 °C. Além disso, a estabilização da enzima nesse suporte permitiu a produção dos seguintes xilooligossacarídeos: xilobiose, xilotriose, xilotetraose e xilopentaose. A purificação da xilanase GH11 foi realizada por meio de uma única etapa cromatográfica de troca catiônica, com rendimento final de 36,72% e um fator de purificação de 7,43 vezes. A massa molecular da enzima foi estimada em 19,5 kDa. Ademais, a sua estrutura tridimensional foi predita por modelagem comparativa, exibindo como modelo final uma arquitetura do tipo ?-jelly roll, comum às xilanases da família 11. Em ensaios de caracterização, a xilanase apresentou melhor atividade em pH 5,5 e manteve atividade residual superior a 80% na faixa de pH compreendida entre 4,0 e 9,0, durante 24 horas. Em relação à temperatura, a sua atividade ótima foi observada a 60 °C, contudo, a sua termoestabilidade foi mais expressiva a 50 °C, retendo cerca de 70% da sua atividade inicial por 480 minutos. Para a xilana beechwood, os valores de velocidade máxima e constante de dissociação aparente foram iguais a 1.330,20 µmol/min/mg e 8,13 mg/mL, respectivamente. Na concentração de 5 mM, os metais pesados Co2+, Hg+, Pb2+ e Zn2+ apresentaram um ponderável efeito de inibição sobre a xilanase GH11, enquanto que os íons Ba2+ e Ni2+, assim como os compostos ?-mercaptoetanol e DTT, exibiram um aumento superior a 20% em sua atividade. Por fim, a análise em tempo real da atividade xilanásica revelou que o substrato xilopentaose corresponde ao menor xilooligossacarídeo capaz de ser eficientemente hidrolisado. Sendo assim, a nova endo-xilanase GH11 isolada do fungo A. tamarii Kita exibe uma série de propriedades físico-químicas favoráveis a sua aplicabilidade em escala industrial. / The endo-1,4-?-xylanases (EC 3.2.1.8) form the largest group of hydrolytic enzymes involved in the degradation of xylan, since they catalyze the random hydrolysis of ?-1,4 glycosidic bonds within the main chain of this polysaccharide, producing xylooligosaccharides of different sizes. In nature, these enzymes are closely related to supplying energy for the development of the organisms that produce them. In general, xylanases are preferentially isolated from bacteria and fungi, which show great potential in industries as brewing, animal feed, food, beverage, xylitol and bioethanol. The present work proposed the isolation of a new endo-1,4-?-xylanase by available techniques of production and purification that can economically make feasible the integration of this biocatalyst to industrial processes. The fungus Aspergillus tamarii Kita, obtained from a soil sample of the Atlantic Forest, showed to be a good xylanase producer in Adams culture medium supplemented with barley bagasse, a byproduct of breweries. After the optimization of the submerged fermentation process, the crude enzymatic extract exhibited two xylanases in activity gel for native proteins, identified by mass spectrometry as glycosyl hydrolases belonging to families 10 and 11. The enzymatic saccharification of three agroindustrial residues, based on an experimental mixture design, showed that the ternary combination of these components, in equal proportions, has considerable relevance for the production of fermentable sugars, such as glucose and xylose. The xylanase GH11 was satisfactorily stabilized on matrices of ionic and covalent character in immobilization assays. Covalent multipoint immobilization on glyoxyl agarose raised its optimum temperature of activity from 60 to 65 °C and offered a considerable gain in thermostability to the derivative, which presented a half-life of 60 minutes at 80 °C. In addition, enzyme stabilization on this support allowed the production of the following xylooligosaccharides: xylobiose, xylotriose, xylotetraose and xylopentaose. Xylanase GH11 purification was carried out by means of a single cation exchange chromatographic step, with final yield of 36.72% and purification factor of 7.43 times. The molecular mass of this xylanase was estimated as 19.5 kDa. Moreover, its three-dimensional structure was predicted by comparative modeling, exhibiting a ?-jelly roll type folding as a final model, common to xylanases of family 11. In characterization tests, xylanase presented better activity at pH 5.5 and was considerably stable in the pH range of 4.0 to 9.0. Regarding temperature, its optimum activity was observed at 60 °C, however, its thermostability was more expressive at 50 °C, retaining about 70% of its initial activity for 480 minutes. In the presence of beechwood xylan, the values of maximum velocity and the constant of apparent dissociation were 1,330.20 µmol/min/mg and 8.13 mg/mL, respectively. At concentrations of 5 mM, the heavy metals Co2+, Hg+, Pb2+ and Zn2+showed an inhibition effect on the xylanase, whereas Ba2+ and Ni2+ ions, as well as ?-mercaptoethanol and DTT, exhibited an increase of more than 20% in their activity. Finally, the real-time analysis of xylanase activity revealed that the xylopentose substrate corresponds to the lowest xylooligosaccharide capable of being hydrolyzed. Thus, the new endo-xylanase GH11 isolated from the fungus A. tamarii Kita exhibits a series of physicochemical properties favorable to its applicability on an industrial scale.

Towards the end of the 7th century A.D., Iraq was in a state of near civil war, caused by social and political malaise. Factional and tribal feuds and fierce antagonism to the Umayyad reign threatened the survival of the dynasty as the unifying force of the empire. Into this situation, al-Ḥasan b. Muḥammad b. al-Ḥanafiyya (d.c. 100/718), a grandson of 'Alī, introduced a peace formula which was intended to pacify the rival religio-political parties. This idea found adherence especially among religious scholars, who quickly broadened its basis, attracting followers to its pacific message. Despite an unstable record of relations with the court, the movement basically supported with its ideology the legitimacy of the Umayyad reign. The popularity of the movement, especially in some scholarly circles in Kufa, led to the formation of a school of religious thought, which had relied on the basic political and religious attitudes of the early Murji'a, but transformed it into a comprehensive theological system. Although not responsible for the actual forging of Murji'ite attitudes, Abū Ḥanīfa had emerged as the eponymous epitome of the movement and the theological school. The first chapter, "Irjā', The Development of the Idea", investigates several possibilities as the source of this notion, among them the alleged Qur'ānic origin, and the Kitāb al-Irjā' attributed to al-Ḥasan b. Muḥammad b. al-Ḥanafiyya. The second chapter, "The Formation of the Murji'a as a ReligioPolitical Movement" surveys the social and the historical background of the Kufan milieu, the formation of the Murji'ite circle and the social elements it was comprised of, and the position of the movement in political and religious affairs in the first two decades of the 8th century .A.D. The third and last chapter, "The Transformation of the Murji'a from a Political into a Religiously-Oriented School" studies and analyses what is believed to be genuine Murji'ite treatises of religious thought, in comparison to sources of a contemporary rival school and the heresiographers. Special emphasis was laid in the analysis on the subject of theology as a medium for political views.

DAKS e.V. ist als Kommunalpolitische Bildungsvereinigung durch das Staatsministerium des Inneren des Freistaats Sachsen anerkannt und steht Bündnis 90/Die Grünen nahe. Sie wurde 1992 auf Anregung der Kommunalpolitischen Konferenz vom Oktober ‘91 in Bautzen gegründet. Ziel ist die „Förderung des demokratischen Staatswesens in weitsichtiger, ökologischer und sozialer Verantwortung. Die Vereinigung unterstützt alle an Kommunalpolitik interessierten Bürgerinnen und Bürger, Abgeordnete, Fraktionen und Bürgerinitiativen bei der Gestaltung einer bürgernahen Kommunalpolitik, welche der Verwirklichung von Menschenrechten, dem Schutz der natürlichen Umwelt und unmittelbaren Bürgerinteressen dient”. Die konkrete Arbeit von DAKS e.V. besteht in Beratung und Schulung von Kommunalpolitikern und interessierten Bürgern mittels Seminaren, Vorträgen und Publikationen sowie in der Vernetzung von Kommunalpolitikern und Fachleuten mittels Tagungen und Vermittlung von Kontakten. Aus den rechtlichen und finanziellen Rahmenbedingungen für Kindertagesstätten sollen Handlungsspielräume für Kommunen abgeleitet werden. Dabei können diese nicht pauschal dargelegt werden, sondern müssen sich in der Kommune an dem tatsächlichen Bedarf und den sozialen Gegebenheiten orientieren.

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