Identification of the metabolites of baicalein in human plasma.

The metabolites of baicalein in human plasma were investigated after taking baicalein, which is one of the main bioactive flavones in Scutellaria baicalensis Georgi. Five metabolites (M1-M5) together with the parent drug baicalein (P) were detected and identified by the HPLC-diode-array detector (DAD) and LC-MS/MS methods. Among them, 7-methoxybaicalein 6-O-glucuronide (M5) is a new metabolite. Based on the results, the proposed metabolic pathway of baicalein in humans was inferred.

Production of l-Methionine from 3-Methylthiopropionaldehyde and O-Acetylhomoserine by Catalysis of the Yeast O-Acetylhomoserine Sulfhydrylase.

l-Methionine is an essential bioactive amino acid with high commercial value for diverse applications. Sustained attentions have been paid to efficient and economical preparation of l-methionine. In this work, a novel method for l-methionine production was established using O-acetyl-homoserine (OAH) and 3-methylthiopropionaldehyde (MMP) as substrates by catalysis of the yeast OAH sulfhydrylase MET17. The OAH sulfhydrylase gene Met17 was cloned from Saccharomyces cerevisiae S288c and overexpressed in Escherichia coli BL21. A 49 kDa MET17 was detected in the supernatant of the recombinant E. coli strain BL21-Met17 lysate with IPTG induction, which exhibited the biological activity of l-methionine biosynthesis from OAH and MMP. The recombinant MET17 was then purified from E. coli BL21-Met17 and used for in vitro biosynthesis of l-methionine. The maximal conversion rate (86%) of OAH to l-methionine catalyzed by purified MET17 was achieved by optimization of the molar ratio of OAH to MMP. The method proposed in this study provides a possible novel route for the industrial production of l-methionine.

The Stability, Microstructure, and Microrheological Properties of Monascus Pigment Double Emulsions Stabilized by Polyglycerol Polyricinoleate and Soybean Protein Isolate.

Monascus pigment is a natural food pigment and is commonly used for coloring and as antiseptic of cured meat products, confectionery, cakes, and beverages. However, Monascus pigment is sensitive to environmental conditions. The main aim of this study was to investigate the effect of polyglycerol polyricinoleate (PGPR) and soy protein isolate (SPI) on the particle size, zeta potential, physical stability, microstructure, and microrheological properties of Monascus pigment double emulsions. The effects of ionic strength, heating, and freeze thawing treatment on the stabilities of Monascus pigment double emulsions were also characterized. It was found that the optimum PGPR and SPI concentrations for fabricating Monascus pigment double emulsion were 3.6 and 3.0 wt%, respectively. The fabricated Monascus pigment double emulsion was composed of fine particles with narrow and uniform size distributions. Microrheological property results suggested that the elastic characteristic of the Monascus pigment double emulsion was dominated with increasing PGPR and SPI contents. It was mainly due to the increased collision and interaction between the droplets during the movement resulting in force increasing. Monascus pigment double emulsions with <5 mM CaCl2 prevented calcium to destroy the physical stability of emulsions, while Monascus pigment double emulsions with more than 10 mM CaCl2 formed creaming. After freeze thawing treatment, creaming occurred in Monascus pigment double emulsion. However, it was stable against heating treatment due to heating leading to a dense network structure. It could be contributed to the practical applications of Monascus pigment double emulsions in food products.

Production of Methionol from 3-Methylthiopropionaldehyde by Catalysis of the Yeast Alcohol Dehydrogenase Adh4p.

Methionol is a sulfur-containing aroma compound that contributes to the flavors of fermented foods. In this work, a novel method for methionol production was established using 3-methylthiopropionaldehyde (MMP) and alcohol dehydrogenase (ADH). First, expression of seven ADH genes was analyzed in yeast fermentation added with MMP. Only ADH4 displayed an evident increased expression in response to MMP. ADH4 was then overexpressed in Saccharomyces cerevisiae S288c and Escherichia coli BL21. The recombinant yeast strain S4 produced more methionol than control strain in MMP fermentation. Furthermore, 0.55 g/L 42 kDa Adh4p was prepared from E. coli by induced expression and purification. A fed-batch catalysis system was finally established to produce methionol from MMP by Adh4p. In 10 h of continuous catalysis, the conversion rate of MMP remained 80-95%, and a final yield of 0.2 g/L methionol was achieved. This work proposed a novel method for methionol production by enzymatic catalysis with a potential application prospect in industry.