Atmospheric cold plasma-assisted pineapple peel waste hydrolysate detoxification for the production of bacterial cellulose.

Toxic compounds in pineapple peel waste hydrolysate (PPWH), namely formic acid, 5-hydroxymethylfurfural (HMF), and furfural, are the major predicament in its utilization as a carbon source for bacterial cellulose (BC) fermentation. A rapid detoxification procedures using atmospheric cold plasma (ACP) technique were employed to reduce the toxic compounds. ACP treatment allows the breakdown of toxic compounds without causing excessive breakdown of sugars. Herein, the performance of two available laboratory ACP reactors for PPWH detoxification was being demonstrated. ACP-reactor-1 (R1) runs on plasma power of 80-200 W with argon (Ar) plasma source, while ACP-reactor-2 (R2) runs at 500-600 W with air plasma source. Treatment in R1, at 200 W for 15 min, results in 74.06%, 51.38%, and 21.81% reduction of furfural, HMF, and formic acid. Treatment in R2 at 600 W gives 45.05%, 32.59%, and 60.41% reductions of furfural, HMF, and formic acid. The BC yield from the fermentation of Komagateibacter xylinus in the R1-treated PPWH, R2-treated PPWH, and untreated-PPWH is 2.82, 3.82, and 2.97 g/L, respectively. The results show that ACP treatment provides a novel detoxified strategy in achieving agricultural waste hydrolysate reuse in fermentation. Furthermore, the results also imply that untreated PPWH can be an inexpensive and sustainable resource for fermentation media supplementation.

Hydrolyzation of mogrosides: Immobilized ß-glucosidase for mogrosides deglycosylation from Lo Han Kuo.

An immobilized enzyme system for bioconversion of Lo Han Kuo (LHK) mogrosides was established. ß-Glucosidase which was covalently immobilized onto the glass spheres exhibited a significant bioconversion efficiency from pNPG to pnitrophenol over other carriers. Optimum operational pH and temperature were determined to be pH 4 and 30°C. Results of storage stability test demonstrated that the glass sphere enzyme immobilization system was capable of sustaining more than 80% residual activity until 50 days, and operation reusability was confirmed for at least 10 cycles. The Michaelis constant (K m) of the system was determined to be 0.33 mM. The kinetic parameters, rate constant (K) at which Mogrosides conversion was determined, the τ 50 in which 50% of mogroside V deglycosylation/mogroside IIIE production was reached, and the τ complete of complete mogroside V deglycosylation/mogroside IIIE production, were 0.044/0.017 min-1, 15.6/41.1 min, and 60/120 min, respectively. Formation of the intermediates contributed to the kinetic differences between mogroside V deglycosylation and mogroside IIIE formation.

Coxsackievirus B3 Induces Autophagic Response in Cardiac Myocytes in vivo.

Viral myocarditis is a common disease that contributes to dilated cardiomyopathy or heart failure. Coxsackievirus B (CVB) is one of the major causative pathogens of viral myocarditis. Previous studies have shown that autophagy is exploited to promote CVB replication in cell lines. To study whether cardiac myocytes respond to CVB infection in a similar way, viral myocarditis was established by the inoculation of 3-week-old BALB/c mice with CVB3. Electron microscopic observation showed that autophagosome-like vesicles were induced in the cardiac myocytes of mice infected by CVB3 at 3, 5, and 7 days after viral infection. The lipidated microtubule-associated protein 1 light chain 3 (LC3), LC3-II, was also significantly increased in both myocardium and the cardiac myocytes extracted from the ventricles of mice infected with CVB3. The increased LC3-II coincided with high level of viral RNA and proteins in both myocardium and isolated cardiac myocytes. Moreover, viral protein synthesis was significantly decreased in primary cardiac myocytes by the treatment with 3-methyladenine, an inhibitor of autophagy. The expression and the phosphorylation of extracellular signal regulated kinase (ERK) were also increased in both myocardium and in the isolated cardiac myocytes of the virus-infected mice, while the interplay of ERK with autophagic response remains to be studied. This study demonstrated that cardiac myocytes respond to CVB3 infection by increased formation of autophagosomes in vivo, which might be exploited for viral replication.