ABSTRACT
BACKGROUND: A series of recently reported phenolic azo dyes 7a-e were prepared by coupling the thienyl diazonium sulfate of 3-Amino-4H-benzo[f]thieno[3,4-c](2H)chromen-4-one with selected diversely substituted phenolic and naphtholic derivatives. These compounds were evaluated for their antibacterial and antifungal activities. Furthermore their voltammetric behavior was compared at a glassy carbon electrode. RESULTS: The voltammetric behavior of the five recently reported azo dyes has been compared at a glassy carbon electrode. It is shown that the azo dyes 7a-e with a hydroxyl group in the ortho position with respect to the azo bridge give rise to well defined, irreversible peaks for the oxidation and reduction process within a pH range of 2-7. The mechanisms of electrochemical oxidation of compound 7a-c and 7e are proposed. For the hydroxyl-substituted dyes, re-oxidation peaks were obtained in the subsequent scan. The antimicrobial activities of the reported compounds 7a-e along with the entire precursors 1-4 and 6a-e were performed against selected bacterial and fungal species and their activities compared to those of nystatin, griseofulvin and ciprofloxacin used as reference drugs. CONCLUSIONS: The present study showed significant antimicrobial activity of compounds 6d, 7a and 7c,e against the tested microorganisms; this result confirms the antimicrobial potency of azo compounds and some of their precursors.
ABSTRACT
Poly(3-hydroxypropionate) (P3HP) is a thermoplastic with great compostability and biocompatibility, and can be produced through several biosynthetic pathways, in which the glycerol pathway achieved the highest P3HP production. However, exogenous supply of vitamin B12 was required to maintain the activity of glycerol dehydratase, resulting in high production cost. To avoid the addition of VB12, we have previously constructed a P3HP biosynthetic route with ß-alanine as intermediate, and the present study aimed to improve the P3HP production of this pathway. L-aspartate decarboxylase PanD was found to be the rate-limiting enzyme in the ß-alanine pathway firstly. To improve the pathway efficiency, PanD was screened from four different sources (Escherichia coli, Bacillus subtilis, Pseudomonas fluorescens, and Corynebacterium glutamicum). And PanD from C. glutamicum was found to have the highest activity, the P3HP production was improved in flask cultivation with this enzyme. To further improve the production, the host strain was screened and the culture condition was optimized. Under optimal conditions, production and content of P3HP reached to 10.2 g/L and 39.1% (wt/wt [cell dry weight]) in an aerobic fed-batch fermentation. To date, this is the highest P3HP production without VB12.
