Scale Development and Model Validation for the Process of Exercise Engagement for People with Prediabetes

Purpose@#This study had two objectives: 1) to develop a scale for the process of exercise engagement (SPEE) for prediabetic individuals (PDIs); 2) to validate a structural model for the process of exercise engagement for PDIs. @*Methods@#A cross-sectional survey with simple random sampling was conducted from September 2013 to December 2015 (in Taiwan). A total of 310 PDIs were enrolled for scale development and model validation via item analysis, factor analyses, and structural equation modeling. The Kuo model was used as the basis for developing the Chinese version of the SPEE for PDIs. @*Results@#The SPEE contains five subscales with a total of twenty-one items that account for 54.9% to 65.9% of the total variance explained for assessing participants’ process of engagement during exercise. For Kuo model validation, the model measures indicated goodness of fit between the Kuo model and sample data. Analysis further revealed a direct effect between the creating health blueprints (CHB) stage and the spontaneous regular exercise (SRE) stage (b=.60). @*Conclusion@#The SPEE includes five subscales for assessing the psychological transition and behavioral expression at each stage of the process of exercise engagement for PDIs. The SPEE for people with prediabetes provides deeper insights into the factors of behavioral change stages that are required to initiate long-term health care outcomes and avoid developing diabetes. These insights are significant as they allow for patient- specific mapping and behavior modification to effect exercise.

Inside a Postpartum Nursing Center: Tradition and Change

PURPOSE: The purpose of this study was to explore how traditional ritual practices are incorporated into the context of contemporary healthcare. METHODS: An ethnographic study was conducted, using observations and interviews with 27 first-time mothers and 3 nurses at a postpartum nursing center in Taipei, Taiwan. RESULTS: Nursing routines, policies and care provision at the center affected the way traditional ritual practices were conducted. New mothers in this study constructed their everyday activities at the center by incorporating and modifying the ritual practices inside and outside the postpartum nursing center setting. CONCLUSIONS: Social changes have an influence on traditional postpartum ritual practices so a postpartum nursing center becomes a choice for postpartum women. Thus, health care professionals should value their own functions and roles at the postpartum nursing center since the new mothers regard them as the primary support resource to help them recover from giving birth. Therefore, they need to re-examine their practices from the postpartum women's perspective to provide better support and sensitive care to postpartum women and their families.

Purification and characterization of an aspartic protease from the Rhizopus oryzae protease extract, Peptidase R

Background Aspartic proteases are a subfamily of endopeptidases that are useful in a variety of applications, especially in the food processing industry. Here we describe a novel aspartic protease that was purified from Peptidase R, a commercial protease preparation derived from Rhizopus oryzae. Results An aspartic protease sourced from Peptidase R was purified to homogeneity by anion exchange chromatography followed by polishing with a hydrophobic interaction chromatography column, resulting in a 3.4-fold increase in specific activity (57.5 × 10³ U/mg) and 58.8% recovery. The estimated molecular weight of the purified enzyme was 39 kDa. The N-terminal sequence of the purified protein exhibited 63-75% identity to rhizopuspepsins from various Rhizopus species. The enzyme exhibited maximal activity at 75°C in glycine-HCl buffer, pH 3.4 with casein as the substrate. The protease was stable at 35°C for 60 min and had an observed half-life of approximately 30 min at 45°C. Enzyme activity was not significantly inhibited by chelation with ethylenediamine tetraacetic acid (EDTA), and the addition of metal ions to EDTA-treated protease did not significantly change enzyme activity, indicating that proteolysis is not metal ion-dependent. The purified enzyme was completely inactivated by the aspartic protease inhibitor Pepstatin A. Conclusion Based on the observed enzyme activity, inhibition profile with Pepstatin A, and sequence similarity to other rhizopuspepsins, we have classified this enzyme as an aspartic protease.