Content: Chamois leathers are basically oil tanned leathers, usually requires 10 to 15 days to process from raw skins. In chamois making, air oxidation plays a major role, free radicals initiate the oxidation process in oil, which oxidizes the double bond of the fatty acid and then the oxidized oil interacts with collagen to stabilize the skin by coating the fibers (Fig 1). In the present study an attempt has been made to reduce the time for chamois leather processing. A common oxidizing agent (Benzoyl peroxide (BPO) was utilized to enhance the oxidation of oil and reduce the time duration. It has been observed that the oxidation of oil in the presence of benzoyl peroxide has significantly reduced the duration of process from 15 to 4 days. Strength properties such as tensile, percentage elongation and organoleptic properties were found to be on par with control leather. The water absorption values of the experimental leathers improved by 1-26 %, compared with control leather. Microscopic analysis (SEM) was employed to study the fiber alignment of the chamois leathers. Take-Away: 1. Time reduction in chamois leather processing 2. Inexpensive and common oxidising agents were employed 3.Improved water absorption of chamois leather

A facile method for the direct conversion of oximes into carbonyl compounds by treatment with manganese triacetate is described. Manganese triacetate can be used for an effective and mild oxidizing agent for the regeneration of carbonyl compounds in good yield. Many functional groups are tolerated under reaction conditions.

Submitted by (edna.saturno@ufrpe.br) on 2017-02-22T13:18:21Z No. of bitstreams: 1 Talita da Silva Esposito.pdf: 1198598 bytes, checksum: 814b0f7dce6420e7e8723706bb578b48 (MD5) / Made available in DSpace on 2017-02-22T13:18:21Z (GMT). No. of bitstreams: 1 Talita da Silva Esposito.pdf: 1198598 bytes, checksum: 814b0f7dce6420e7e8723706bb578b48 (MD5) Previous issue date: 2006-02-06 / Alkaline proteases are commercially important group of enzymes and have a large variety of applications, mainly in the detergent and food industries. The proteases currently uses in the market are serine proteases produced by Bacillus strains, principally. Fish viscera have wide biotechnological potential as a source of digestive proteases. Biotechnology provides a means for transforming such materials usually discarded into valuable produts such as enzymes. The objective of this research was to test if alkaline proteases from fish viscera could be used as an additive in commercially available detergent formulations. Viscera from Colossoma macropomum, the most important native fish for Brazilian aquaculture, and Cyprinus carpio, the second exotic fish in importance for Brazilian aquaculture, were extracted and used as a source of enzyme for this research. The crude extract obtained upon the homogenization of the viscera was submitted to a partial purification with ethanol. The protein content,proteolytic activity of the fractions thus obtained was assessed. The fraction presenting the highest proteolytic activity was further studied (30-70% of ethanol) resulting in 74.9% and 142.4% of protein recovery for tambaqui and carpa, respectively. This fraction was assayed at different temperatures and pH aiming to estimate the conditions for higher proteolysis. Temperarture and pH stability experiments were also carried out. Different commercial lyavailable detergents, surfactants and hydrogen peroxide were used to test the compatibility of these proteases with detergent formulations. The results reveal that these alkaline proteases extracted from C. macropomum show desirable characteristics for its use in laundry industry such as: retention of 73% and 63% of its initial activity in the presence of Surf® and 5% H202, respectively, after 1 hour of incubation at 40ºC. In addition to that it was observed a slight increase of the proteolytic activity in the presence of non-ionic (Tween 20 and Tween 80) and ionic surfactants (Saponin and Sodium cholate). On the other hand, the proteases extracted from the intestine of C. carpio were compatible with the surfactants and oxidants tested butdid not present the same property in the presence of commercially available detergents. / As proteases alcalinas são as enzimas de maior importância comercial devido a sua vasta aplicabilidade, sendo empregadas principalmente nas indústrias de detergentes e de alimentos. Atualmente, a maior parte das proteases utilizadas no mercado é produzida por bactérias do gênero Bacillus, no entanto, elas podem ser amplamente encontradas em um dos principais resíduos da indústria pesqueira, as vísceras. Portanto, uma forma de otimizar o aproveitamento do pescado e, conseqüentemente, reduzir o desperdício é reaproveitar esses subprodutos. Neste trabalho testou-se a aplicabilidade das proteases de vísceras de peixes como aditivo de detergentes em pó comerciais. Para extração das enzimas foram utilizadas vísceras de Colossoma macropomum e de Cyprinus carpio, principal peixe nativo e segundo peixe exótico da aqüicultura continental nacional, respectivamente. A partir deste material obteve-se o extrato bruto, que passou por uma semi-purificação fracional com etanol. As frações obtidas deste procedimento tiveram sua atividade enzimática e quantidade de proteínas determinadas para escolha da fração a ser trabalhada. A fração saturada com 30- 70% de etanol apresentou maior atividade específica tanto no tambaqui quanto na carpa, com rendimentos de 74,9% e 142,4%, respectivamente. Nesta fração verificou-se em que temperatura e pH as proteases apresentavam maior atividade, além da sua estabilidade em relação a esses parâmetros. Para testar a compatibilidade com detergentes comerciais, foram utilizados quatro detergentes comerciais, cinco agentes surfactantes e peróxido de hidrogênio em diferentes concentrações. Os resultados obtidos sugerem que as proteases alcalinas encontradas nas vísceras de tambaqui apresentam características ideais para utilização na indústria de detergentes em pó, como: retenção de até 73% da sua atividade na presença de Surf® e de 63% na presença de 5% de H2O2 após 1 hora de incubação a 40ºC. Além disso, a atividade da enzima foi estimulada na presença de surfactantes não-iônicos (Tween 20 e Tween 80) e iônicos (Saponin e Colato de sódio). As proteases obtidas a partir do intestino da carpa, no entanto, só foram estáveis na presença dos diferentes surfactantes e a 5% de H2O2, perdendo estabilidade quando adicionadas aos detergentes comerciais.