4,285 research outputs found

    Sistema de produção de bubalinos para leite e carne.

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    Iogurte de leite de bĂșfala com sabores de frutas da AmazĂŽnia.

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    bitstream/item/33778/1/CPATU-CirTec23.pd

    CaracterĂ­sticas, peculiaridades e tecnologia do leite de bĂșfala.

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    CaracterĂ­sticas e peculiaridades do leite de bĂșfala. Industrialização do leite. CaracterĂ­sticas dos produtos derivados do leite de bĂșfala. Tecnologia do leite de bĂșfala e rendimento dos produtos.bitstream/item/58474/1/CPATU-DOC-57-.pd

    Fast analysis of low molecular mass compounds present in snake venom: identification of ten new pyroglutamate-containing peptides.

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    Made available in DSpace on 2018-06-09T01:20:56Z (GMT). No. of bitstreams: 1 ID25295.pdf: 254192 bytes, checksum: 13faf75f59f61e212f0e82fe521da5d8 (MD5) Previous issue date: 2005-07-21bitstream/item/178385/1/ID-25295.pd

    Suplementação mineral de bovinos de corte em pastagem nativa.

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    bitstream/item/33524/1/CPATU-CirTec12.pd

    Kinetics of b-galactosidase immobilized on polysiloxanepolyvinyl alcohol magnetic composite – POS-PVAM

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    b-Galactosidase is an enzyme with a wide industrial application, mostly in the hydrolysis of lactose and, more recently, in the synthesis of oligosaccharides. Several advantages are associated with the application of immobilized enzymes. In this work, b-Galactosidase was covalently immobilized onto a POS-PVAM using glutaraldehyde as activating agent and its hydrolytic properties evaluated. For both soluble and immobilized b-Galactosidase, the optimal temperature and pH were found to be 50 ÂșC and 6.5, respectively. The immobilized enzyme showed to be more resistant than the soluble form when hydrolysis experiments were performed out within the above optimal condition, being the observed difference in activity more pronounced for temperatures higher than 50ÂșC. An enhancement of the thermal stability of the immobilized enzyme was also observed. The apparent Km and Ea for both soluble (7.377 ± 1.303mM and 25.51 ± 8.72Kj mol-1) and immobilized enzyme (7.841 ± 1.189mM and 32.61 ± 5.82Kj mol-1) showed to be not significantly different. The immobilization also proved to be advantageous as, after twenty reutilizations, the immobilized enzyme retained about 52% of its initial activity. These results clearly demonstrate that POS-PVAM may be used for b- Galactosidase immobilization since, besides improving the enzyme hydrolytic properties, its separation from the obtained reaction products is easier to accomplish

    CaracterĂ­sticas de carcaças de bĂșfalos engordados em pastagem nativa de terra inundĂĄvel.

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    Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis

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    ÎČ-Galactosidase from Kluyveromyces lactis was covalently immobilized onto a mPOS–PVA, using glutaraldehyde as activating agent and its properties were evaluated. The enzymatic water insoluble derivative displayed the same optimum pH (6.5) and optimum temperature (50 °C) of the soluble enzyme. The apparent Km app and activation energy for both soluble and immobilized enzyme derivative were found to be not significantly different. The mPOS–PVA ÎČ-galactosidase preparation presented a higher operational and thermal stability than the soluble enzyme. This immobilized ÎČ-galactosidase also was effective in hydrolyzing lactose from milk. Hence, one can conclude that mPOS–PVA is an attractive and efficient support for ÎČ-galactosidase immobilization.Alban, the European Union Programme of High Level Scholarships for Latin America; Brazilian National Research Council (CNPq)
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