Mycoplasma pneumoniae(MP) is a leading pathogen of respiratory infection, especially community-acquired pneumonia (CAP), in children worldwide. However, its diagnosis is frequently ineffective because bacterial culture and serology test are usually positive 1–2 weeks or more after the disease onset. To achieve a better detection efficiency, the single-walled carbon nanotubes(SWCNT) were coupled with the colloidal gold-monoclonal antibody immunochromatographic strips(CGIC). Interestingly, the SWCNT/CGIC assay allowed MP identification, with a detection limit of 1 × 102 copies/ml. Using referenced throat swabs of 97 MP and 40 non-MP cases, the assay yielded 72.2% sensitivity, 100.0% specificity, 100.0% positive predictive value (PPV), 59.7% negative predictive value (NPV). In summary, our assay was far more effective than any conventional methods for the diagnosis of acute MP. The ease of use, rapid and stability further enhance its feasibility for clinical use on-site.

To explore the potential metabolites from rabeprazole sulfide, seven strains of filamentous fungi were screened for their biotransformation abilities. Among these strains, Cunninghamella blakesleeana 3.970 exhibited the best result. Four different culture media were screened in order to identify the most optimal for subsequent research. Single factors such as the initial pH of culture media, culture time, inoculation volume, and media volume were individually investigated to provide the optimum biotransformation conditions. Then, an orthogonal optimization process using a five-factor, four-level L16(45) experiment was designed and performed. Finally, when the substrate concentration is 3 g/L, one major metabolite was detected with a transformation rate of 72.4%. Isolated by semipreparative HPLC, this metabolite was further detected by ESI-MS and NMR. The final data analysis indicated that the metabolite is O-demethylation rabeprazole sulfide.

Streptomyces noursei D-3-14 was taken as a starting strain and treated with UV (15 W, 30 cm) mutagenesis for 40 s for three consecutive rounds. High yielding strains were screened using chemical and biological potency determination, and the components of the fermentation products were detected using HPLC. Finally, the mutant strain Streptomyces noursei 72-22-1 with a chemical potency of 8912 (U/mL) and a biological potency of 5557 (U/mL) was obtained after the genetic stability evaluation. After optimization of the fermentation conditions, the chemical potency and biological potency of Streptomyces noursei 72-22-1 reached 14,082 U/mL and 10579 U/mL, respectively, which is 1.58 and 1.91 times those before optimization. HPLC analysis indicated that the mutant strain 72-22-1 displayed a higher content of polyfungin B. When equimolar nystatin A1, A3, and polyfungin B were tested for their fungicidal activities towards Saccharomyces cerevisiae ATCC 2061, polyfungin B exhibited a better efficacy than nystatin A1 and A3.

The hydroxylation of dehydroepiandrosterone (DHEA) to 7α -hydroxy-5-androstene-17-one (7α-OH-DHEA) and 7β-hydroxy-5-androstene-17-one (7β-OH-DHEA) by Gibberella sp. CICC 2498 and Absidia coerulea CICC 41050 was investigated. The media ingredients were optimized. Single factors such as the DHEA concentration, culture time, medium volume, and inoculum rate were individually investigated to generate optimum biotransformation conditions. An orthogonal optimization process using a four-factor, three- level L9 (33) experiment was designed and performed. Finally, the maximum production of 7β-OH-DHEA from DHEA biotransformation by Absidia coerulea is 69.61%. This strategy would provide a possible way to enhance the 7β-OH-DHEA yield in the pharmaceutical industry.

Free enzymes often face economic problems because of their non-repeatability and variability, which limit their application in industrial production. In this study, KDN lipase was immobilized with the macroporous resin LXTE-1000 and glutaraldehyde. The optimal conditions of enzyme immobilization were defined by a single factor experiment and response surface methodology (RSM). The concentration of the cross-linking agent glutaraldehyde was 0.46% (v/v), the cross-linking temperature was 25.0 °C, and the cross-linking time was 157 min. The enzyme activity of the immobilized KDN lipase after adsorption/cross-linking was 291.36 U/g, and the recovery of the enzyme activity was 9.90%. The optimal conditions for the synthesis of isopropyl myristate were catalyzed by the immobilized KDN lipase in a solvent-free system: immobilized enzyme 53 mg, reaction temperature 36.1 °C, myristic acid 228.4 mg, isopropanol 114 µL, and reaction time 18 h. The yield of isopropyl myristate was 66.62%. After ten cycles, the activity of the immobilized KDN lipase preserved more than 46.87% of its initial enzyme activity, and it demonstrated high tolerance to solvents compared to free KDN lipase.