Clinical study on polycystic ovary syndrome treated with Diane-35 and Pioglitazone.

OBJECTIVE: To observe the effects of Diane-35 and pioglitazone on endocrine, blood lipid, and blood glucose metabolism in patients with polycystic ovary syndrome (PCOS). METHODS: 70 PCOS patients were selected as subjects between January 2019 and January 2020 and were randomized into two groups. The control group was provided with Diane-35 for 1 tablet/day. The patients in the observation group took additional pioglitazone twice a day. The therapeutic effect of the two schemes was analyzed by observing hormone, blood lipid, and blood glucose levels. The body mass index (BMI), waist-hip ratio (WHR), and Ferriman-Gallwey score (F-G) of the two groups of patients at different time points were compared. RESULTS: Compared with the control group, after pioglitazone treatment, a significant decrease was observed in the levels of various hormone factors. In the observation group (all P<0.01) and the observation group yielded lower levels of fasting blood glucose (FBG), fasting insulin (FIN), Homeostatic Model Assessment for Insulin Resistance (Homa IR), and Homeostatic Model Assessment for ß-cell function (Homa B), as compared to the control group (all P<0.01). Additionally, compared with the control group, the high-density lipoprotein (HDL) levels in the observation group saw a spike (P<0.01). The low-density lipoprotein (LDL) levels witnessed a downturn (P<0.01). Immediately after treatment and 1 month after treatment, the BMI, WHR, and F-G scores of the two groups declined gradually, with lower WHR and F-G scores of the observation group than those of the control group (P<0.01). CONCLUSION: Diane-35 and pioglitazone can effectively improve the symptoms of sex hormone secretion, blood glucose, and blood lipid disorder in PCOS patients, which has high clinical application value.

A Novel Digestive GH16 ß-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi.

ß-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted ß-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 ß-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo ß-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive ß-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry.

[Molecular modification of ß-glucosidase from the midgut of Macrotermes barneyi].

Cellulose hydrolysis to glucose requires a series of cellulase enzymes, of which ß-glucosidases play a crucial role. ß-glucosidase (MbmgBG1) derived from the midgut of Macrotermes barneyi has higher glucose tolerance (maintaining more than 60% enzyme activity at 1.5 mol/L glucose). However, low enzyme activity and poor thermal stability limit the applications of ß-glucosidase in food industries. Point mutants (F167L, T176C, E347I, R354K, N393G and V425M) were obtained by site-directed mutagenesis of non-conserved amino acids near conserved amino acids. Among them, the specific activities against to substrate pNPG of two mutants (F167L and R354K) were about 2-fold and 4-fold higher than that of MbmgBG1. Kcat/Km values were also higher than that of the wild-type, reflecting stronger affinity to the substrate and higher catalytic ability of mutants than MbmgBG1. When the glucose concentration was 1.5 mol/L, the enzyme activity of MbmgBG1 was about 60% of the original activity. F167L and R354K kept 60% enzymatic activity when the glucose concentrations of was 2.0 mol/L and 3.0 mol/L, respectively. These results lay a foundation for further studies on the catalytic efficiency of ß-glucosidase.