A gene coding for a thermostable esterase was isolated by functional screening of Escherichia coli cells that had been transformed with fosmid environmental DNA libraries constructed with metagenomes from thermal environmental samples. The gene conferring esterase activity on E. coli grown on tributyrin agar was composed of 936 bp, corresponding to 311 amino acid residues with a molecular mass of 34 kDa. The enzyme showed significant amino acid similarity (64%) to the enzyme from a hyperthermophilic archaeon, Pyrobaculum calidifontis . An amino acid sequence comparison with other esterases and lipases revealed that the enzyme should be classified as a new member of the hormone-sensitive lipase family. The recombinant esterase that was overexpressed and purified from E. coli was active above 30°C up to 95°C and had a high thermal stability. It displayed a high degree of activity in a pH range of 5.5 to 7.5, with an optimal pH of approximately 6.0. The best substrate for the enzyme among the p -nitrophenyl esters (C ₄ to C ₁₆ ) examined was p -nitrophenyl caproate (C ₆ ), and no lipolytic activity was observed with esters containing an acyl chain length of longer than 10 carbon atoms, indicating that the enzyme is an esterase and not a lipase.

In a fluorescence polarization screen for the MYC–MAX interaction, we have identified a novel small-molecule inhibitor of MYC, KJ-Pyr-9, from a Kröhnke pyridine library. The K_d of KJ-Pyr-9 for MYC in vitro is 6.5 ± 1.0 nM, as determined by backscattering interferometry; KJ-Pyr-9 also interferes with MYC–MAX complex formation in the cell, as shown in a protein fragment complementation assay. KJ-Pyr-9 specifically inhibits MYC-induced oncogenic transformation in cell culture; it has no or only weak effects on the oncogenic activity of several unrelated oncoproteins. KJ-Pyr-9 preferentially interferes with the proliferation of MYC-overexpressing human and avian cells and specifically reduces the MYC-driven transcriptional signature. In vivo, KJ-Pyr-9 effectively blocks the growth of a xenotransplant of MYC-amplified human cancer cells.

Kimchi is a fermented food prepared via spontaneous fermentation by lactic acid bacteria originating from raw ingredients. To investigate the effect of these ingredients on food fermentation, four types of food that differed only in their main raw ingredients (kimchi cabbage, green onion, leaf mustard, and young radish) were evaluated. The major microorganisms were Leuconostoc gelidum, Weissella kandleri, and Lactobacillus sakei groups. The distribution of these species depended on the sample type. All three species were primarily distributed in the food prepared from kimchi cabbage and young radish; however, the Lac. sakei group was hardly found in the food prepared using green onion and leaf mustard. Metabolite analysis results showed that the free sugar, organic acid, ethanol, and amino acid profiles differed with the sample type. This study indicates that the main ingredients could be an important factor in determining the composition of the microbial community and the metabolite composition.