1,207 research outputs found

    Development and validation of a scale to measure social isolation in adolescents

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    Background: There is a lack of questionnaires specifically designed to assess social isolation in adolescents. We developed and validated a self-report measure of social isolation in adolescents, the Social Isolation Questionnaire (QIS). Methods: A literature review on social isolation and mental health in adolescents indicated 20 questions to form QIS. Two cross-sectional surveys with 48 and 1,135 adolescents, respectively, evaluated the reproducibility and validity of QIS. Results: The Bland-Altman plot did not indicate a systematic difference between measurements 15 days apart. Bartlett’s sphericity test verified a correlation between the questions and the Kaiser-Meyer-Olkin test showed good adequacy (0.896) to the factor analysis. Exploratory factor analysis suggested the exclusion of three questions (loading factors <0.3), and eigenvalues (4.9 to 0.8) indicated that the questionnaire should be composed of three factors (dimensions). The Cronbach’s alpha indicated high internal consistency of the 17 questions (0.850 overall; Dimensions: 0.815 ‘feeling of loneliness’; 0.760 ‘friendship’; and, 0.680 ‘Family support’). The QIS score ranged from 0 to 131 (maximum social isolation score). Correlation between QIS and depressive symptoms (r=0.543) indicated the construct validity of QIS. Limitations: We evaluated QIS in the Portuguese version, thus translation and cultural adaptation are necessary to evaluate the questionnaire in other settings. Conclusions: We constructed and validated the QIS questionnaire, a self-administered questionnaire to assess social isolation in adolescents, composed of three dimensions; feeling of loneliness, friendship and family support. The QIS questionnaire seems a very promising tool to support practitioners and researchers in assessing social isolation among adolescents

    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

    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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