BackgroundOne of the most important challenges in public health is to improve the quality of life in patients with chronic heart failure (CHF). Depression, self-care capacity, and quality of life interact each other in these patients. It’s difficult to treat with general education programs and conventional therapy. PRECEDE model is a comprehensive and exclusive theory-based education programs. Its effectiveness for reducing depression and increasing quality of life has been demonstrated in patients with coronary artery bypass grafting, type 2 diabetes, and the elderly. It has not been used in elderly patients with CHF. Thus, this study aims to investigate the effects of this model on self-care behaviors, depression, and quality of life in these patients.MethodsPatients who met the inclusion criteria were randomly assigned to the intervention or control group. All the patients received conventional medical care. The patients in the intervention group also received 9 sessions of education intervention based on the PRECEDE model and then followed up for 3 months after the intervention. Data were collected before and 3 months after the intervention using 4 questionnaires, namely a PRECEDE-based questionnaire to evaluate predisposing, reinforcing, and enabling factors; the 9-item European Heart Failure Self-care Behavior Scale (EHFScBS-9); the 9-item Personal Health Questionnaire (PHQ-9); and the Minnesota Living with Heart Failure Questionnaire (MLHFQ).ResultsNo significant differences were found in the mean scores for the predisposing, enabling, and reinforcing factors, and the mean total scores in EHFScBS-9, PHQ-9, and MLHFQ before the intervention between the intervention and control groups. After the intervention, the scores for the predisposing, reinforcing, and enabling factors increased significantly, and the mean total scores in EHFScBS-9, PHQ-9, and MLHFQ decreased significantly in the intervention group. In addition, these scores significantly differed from those of the control group. Furthermore, the MLHFQ score significantly correlated with the EHFScBS-9 and PHQ-9 scores.ConclusionThis study demonstrates a trend that PRECEDE model of health education promotion is effective in relieving depression symptoms, enhancing self-monitoring, and improving the quality of life of elderly patients with CHF.Trial registrationTrial registration number: ChiCTR-IOR-17012779; Trial registry: Chinese Clinical Trial Registry; Date registered: 22 Sep 2017; Retrospectively registered.

The widely used plasticizer phthalate esters (PAEs) have become a public concern because of their effects on environmental contamination and toxicity on mammals. However, the biodegradation of PAEs, especially diisobutyl phthalate (DiBP), remains poorly understood. In particular, genes involved in the hydrolysis of these compounds were not conclusively identified. In this study, the CarEW gene, which encodes an enzyme that is capable of hydrolyzing ρ-nitrophenyl esters of fatty acids, was cloned from a thermophilic bacterium Bacillus sp. K91 and heterologously expressed in Escherichia coli BL21 using the pEASY-E2 expression system. The enzyme showed a monomeric structure with a molecular mass of approximately 53.76 kDa and pI of 4.88. The enzyme exhibited maximal activity at pH 7.5 and 45°C, with ρ-NP butyrate as the best substrate. The enzyme was fairly stable within the pH range from 7.0 to 8.5. High-pressure liquid chromatography (HPLC) and electrospray ionization mass spectrometry (ESI-MS) were employed to detect the catabolic pathway of DiBP. Two intermediate products were identified, and a potential biodegradation pathway was proposed. Altogether, our findings present a novel DiBP degradation enzyme and indicate that the purified enzyme may be a promising candidate for DiBP detoxification and for environmental protection.

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Mining for novel enzymes from new microorganisms is a way to obtain β-xylosidases with promising applications. A Sphingomonas β-xylosidase was expressed in Escherichia coli. The purified recombinant enzyme (rJB13GH39) was most active at pH 4.5 and 50 °C, retaining 10%-50% of its maximum activity at 0-20 °C. Most salts and chemical reagents including 3.0%-20.0% (w/v) NaCl showed little or no effect on the enzymatic activity. rJB13GH39 exhibited 71.9% and 55.2% activity in 10.0% and 15.0% (v/v) ethanol, respectively. rJB13GH39 was stable below 60 °C in 3.0%-30.0% (w/v) NaCl, 3.0%-20.0% (v/v) ethanol, and 2.2-87.0 mg/mL trypsin. The enzyme transferred one xylosyl moiety to certain sugars and alcohols. The salt/ethanol tolerance and low-temperature activity of the enzyme may be attributed to its high structural flexibility caused by high proportions of small amino acids ACDGNSTV and random coils.