Biobutanol can be produced by Clostridia via an acetone–butanol–ethanol (ABE) fermentation under strictly anaerobic conditions. Oxygen-free nitrogen (OFN) gas is typically used to create anaerobic conditions for ABE fermentations. However, this method is not appropriate for large-scale fermentations as it is quite costly. The aim of this work was to study the feasibility of butanol production from sweet sorghum juice (SSJ) by Clostridium beijerinckii TISTR 1461 using various methods to create anaerobic conditions, i.e., growth of a strictly aerobic bacterium, an Arthrobacter sp., under different conditions and a chemical method using sodium dithionite (SDTN) to consume residual oxygen. SSJ containing 60 g/L of total sugar supplemented with 1.27 g/L of (NH4)2SO4 was used as a substrate for butanol production. The results showed that 0.25 mM SDTN could create anaerobic conditions, but in this case, C.beijerinckii TISTR 1461 could produce butanol at a concentration (PB) of only 8.51 g/L with a butanol productivity (QB) of 0.10 g/L·h. Arthrobacter sp. BCC 72131 could also be used to create anaerobic conditions. Mixed cultures of C.beijerinckii TISTR 1461 and Arthrobacter sp. BCC 72131 created anaerobic conditions by inoculating the C.beijerinckii 4 h after Arthrobacter. This gave a PB of 10.39 g/L with a QB of 0.20 g/L·h. Comparing butanol production with the control treatment (using OFN gas to create anaerobic conditions, yielding a PB of 9.88 g/L and QB of 0.21 g/L·h) indicated that using Arthrobacter sp. BCC 72131 was an appropriate procedure for creating anaerobic conditions for high levels of butanol production by C. beijerinckii TISTR 1461 from a SSJ medium.

Vibrio spp. play a vital role in the recycling of chitin in oceans, but several Vibrio strains are highly infectious to aquatic animals and humans. These bacteria require chitin for growth; thus, potent inhibitors of chitin-degrading enzymes could serve as candidate drugs against Vibrio infections. This study examined NAG-thiazoline (NGT)-mediated inhibition of a recombinantly expressed GH20 b-N-acetylglucosaminidase, namely VhGlcNAcase from Vibrio campbellii (formerly V. harveyi) ATCC BAA-1116. NGT strongly inhibited VhGlcNAcase with an IC 50 of 11.9 AE 1.0 lM and K i 62 AE 3 µM, respectively. NGT was also found to completely inhibit the growth of V. campbellii strain 650 with an minimal inhibitory concentration value of 0.5 µM. ITC data analysis showed direct binding of NGT to VhGlcNAcase with a K d of 32 AE 1.2 lM. The observed DG°b inding of À7.56 kcalÁmol À1 is the result of a large negative enthalpy change and a small positive entropic compensation, suggesting that NGT binding is enthalpy-driven. The structural complex shows that NGT fully occupies the substrate-binding pocket of VhGlcNAcase and makes an exclusive hydrogen bond network, as well as hydrophobic interactions with the conserved residues around the À1 subsite. Our results strongly suggest that NGT could serve as an excellent scaffold for further development of antimicrobial agents against Vibrio infections.

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