Navegando por Palavras-chave "beta-glucosidase"

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    Biochemical Characterization of an In-House Coccidioides Antigen: Perspectives for the Immunodiagnosis of Coccidioidomycosis
    (Mdpi Ag, 2012-07-01) Moreira Filho, Renato Evando; Bandeira, Silviane Praciano; Nogueira Brillhante, Raimunda Samia; Gadelha Rocha, Marcos Fabio; Vasconcelos, Ilka Maria; Pereira, Mirella Leite; Collares Maia Castelo-Branco, Debora de Souza; Castro Rocha, Francisco Airton; Camargo, Zoilo Pires de [UNIFESP]; Ramos, Marcio Viana; Cordeiro, Rossana de Aguiar; Costa Sidrim, Jose Julio; Univ Fed Ceara; Univ Estadual Ceara; Universidade Federal de São Paulo (UNIFESP)
    The objective of this study was to evaluate the reactivity of an in-house antigen, extracted from a strain of C. posadasii isolated in northeastern Brazil, by radial immunodiffusion and Western blotting, as well as to establish its biochemical characterization. the protein antigen was initially extracted with the use of solid ammonium sulfate and characterized by 1-D electrophoresis. Subsequently, it was tested by means of double radial immunodiffusion and Western blotting. A positive reaction was observed against the antigen by both immunodiagnostic techniques tested on sera from patients suffering from coccidioidomycosis. Besides this, two immunoreactive protein bands were observed and were revealed to be a beta-glucosidase and a glutamine synthetase after sequencing of the respective N-terminal regions. Our in-house Coccidioides antigen can be promising as a quick and low-cost diagnostic tool without the risk of direct manipulation of the microorganism.
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    Lactobacillus fermentation of jussara pulp leads to the enzymatic conversion of anthocyanins increasing antioxidant activity
    (Academic Press Inc Elsevier Science, 2018) Braga, Anna Rafaela Cavalcante [UNIFESP]; Mesquita, Leonardo Mendes de Souza [UNIFESP]; Martins, Paula Larangeira Garcia [UNIFESP]; Habu, Sascha [UNIFESP]; Rosso, Veridiana Vera de [UNIFESP]
    Bacteria possessing an enzymatic system able to metabolize anthocyanins may play a major role in the production of compounds with different bioavailability and biological activity. In this study, Lactobacillus and Bifidobacterium strains were screened for the enzymatic activities of alpha-galactosidase, beta-galactosidase and beta-glucosidase. These strains were also screened for their ability to convert the anthocyanins from jussara. The nine evaluated strains produced at least two of the three enzymes
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    A Novel beta-Glucosidase from Sporidiobolus pararoseus: Characterization and Application in Winemaking
    (Wiley-Blackwell, 2011-09-01) Baffi, Milla Alves; Tobal, Thaise; Lago, Joao Henrique G. [UNIFESP]; Leite, Rodrigo S. R.; Boscolo, Mauricio; Gomes, Eleni; Da-Silva, Roberto; Universidade Federal de Uberlândia (UFU); Universidade Federal de São Paulo (UNIFESP); Univ Fed Grande Dourados UFGD; São Paulo State Univ UNESP
    For the first time, the production of an extracellular beta-glucosidase (Sp-beta-gl) by a Sporidiobolus pararoseus yeast strain is reported. the Sp-beta-gl activity was quantified, characterized, and assessed for its efficiency in releasing aroma-enhancing compounds in wines. the maximum enzymatic synthesis was after 72 h of growth in a complex media with 20 g/L of cellobiose. the optimal pH and temperature were 5.5 and at 50 degrees C, respectively. It showed a wide range of pH stability and exhibited quite high thermostability at low temperatures. in addition, this beta-glucosidase revealed tolerance to wine-associated inhibitory compounds (sugars and ethanol), showing suitable characteristics for all the stages of alcoholic fermentation. the hydrolysis of the glycosidic terpenes by Sp-beta-gl was studied by gas chromatography, and its ability to efficiently release free terpenols has been demonstrated. the concentrations of geraniol, linalool, alpha-terpineol, and nerol were significantly increased in treated wines. These results suggest the potential application of this new yeast beta-glucosidase as an aroma-enhancing enzyme in winemaking.