Hydrolyzed Rice Protein
Mostrando 1-4 de 4 artigos, teses e dissertações.
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1. Hydrolysis of various thai agricultural biomasses using the crude enzyme from Aspergillus aculeatus iizuka FR60 isolated from soil
In this study, forty-two fungi from soil were isolated and tested for their carboxymethyl cellulase (CMCase) and xylanase activities. From all isolates, the fungal isolate FR60, which was identified as Aspergillus aculeatus Iizuka, showed high activities in both CMCase and xylanase with 517 mU/mg protein and 550 mU/mg protein, respectively. The crude enzyme
Brazilian Journal of Microbiology. Publicado em: 2012-06
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2. Estabilidade de formulações cosméticas antienvelhecimento com hidrolisado de proteína do arroz (Oryza sativa) / Stability of cosmetic formulations with aging hydrolyzed protein in rice (Oryza sativa)
O hidrolisado de proteína do arroz (Oryza sativa) apresenta à habilidade de aumentar à produção de fibroblastos e colágeno, devido a esta especificidade, cada vez mais a indústria cosmética mostra interesse em utilizar peptídeos como ativo de suas formulações.O presente trabalho tem como objetivo a avaliação da estabilidade de formulações cosm
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 21/09/2011
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3. Energetic and protein diet for adults of Apis mellifera Linnaeus 1758 (Hymenoptera: Apidae). / Dietas energÃticas e protÃicas para adultos de Apis mellifera Linnaeus, 1758 (Hymenoptera: Apidae)
The diet fed to adults of Apis mellifera in confinement is a relevant factor in the survival of these insects. In times of nectar shortage, a feeding supplementation with a solution of hydrolyzed sucrose through acid and heating can be given to the hive; citric acid found in lemon juice could be used. In this research, the survival of these confined insects
Publicado em: 2008
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4. Identification, Purification, and Characterization of a Thermally Stable Lipase from Rice Bran. A New Member of the (Phospho) Lipase Family1
A thermally stable lipase (EC 3.1.1.3.) was first identified in rice (Oryza sativa) bran, and the enzyme was purified to homogeneity using octyl-Sepharose chromatography. The enzyme was purified to 7.6-fold with the final specific activity of 0.38 μmol min−1 mg−1 at 80°C using [9,10-3H]triolein as a substrate. The purified enzyme was found to be a glyc
American Society of Plant Physiologists.