• Food Science and Preservation
• /
• v.15 no.4
• /
• pp.532-541
• /
• 2008

A central composite design was applied to investigate the effects of the independent variables of NaOH concentration(X1) and extraction time(X2) on dependent variables such as Yield(Y1), Xyl/Ara ratio(Y2), uronic acid(Y3), $\beta$-glucan(Y4) and total sugars(Y5) of hemicelluloses separated from rice bran. The Coefficients of determination(R2) in various models ranged from 0.8626 to 0.9319. Yield increased with increased NaOH concentration and extraction time. The optimum extraction conditions were NaOH concentration at 2.45M and extraction time of 24.2 h. Predicted values at the optimized conditions were acceptable, compared with experimental values. The structural characteristics of an optimum hemicellulose extract were explored. As a result, it showed that the surfaces of hemicellulose had a highly irregular reticulated structure. And also it was both small and large molecular particle in the hemicelluloses. Their average molecular weights were in the ranges $235{\sim}240$ kDa and $8.0{\sim}9.4kDa$, respectively.

• Journal of Microbiology
• /
• v.43 no.spc1
• /
• pp.110-117
• /
• 2005

Salmonella enterica serovar Typhimurium causes human gastroenteritis and a systemic typhoid-like infection in mice. A critical virulence determinant of Salmonella is the ability to invade mammalian cells. The expression of genes required for invasion is tightly regulated by environmental conditions and a variety of regulatory genes. The hilA regulator encodes an OmpR/ToxR family transcriptional regulator that activates the expression of invasion genes in response to both environmental and genetic regulatory factors. Work from several laboratories has highlighted that regulation of hilA expression is a key point for controlling expression of the invasive phenotype. A number of positive regulators of hilA expression have been identified including csrAB, sirA/barA, pstS, hilC/sirC/sprA, fis, and hilD. HilD, an AraC/XylS type transcriptional regulator, is of particular importance as a mutation in hilD results in a 14-fold decrease in chromosomal hilA::Tn5lacZY-080 expression and a 53-fold decrease in invasion of HEp-2 cells. It is believed that HilD directly regulates hilA expression as it has been shown to bind to hilA promoter sequences. In addition, our research group, and others, have identified genes (hilE, hha, pag, and lon) that negatively affect hilA transcription. HilE appears to be an important Salmonella-specific regulator that plays a critical role in inactivating hilA expression. Recent work in our lab has been directed at understanding how environmental signals that affect hilA expression may be processed through a hilE pathway to modulate expression of hilA and the invasive phenotype. The current understanding of this complex regulatory system is reviewed.

• Journal of Microbiology
• /
• v.35 no.4
• /
• pp.300-308
• /
• 1997

The catechol 2,3-dioxygenase (C23O) encoded by the Pseudomonas putida xylE gene was over-produced in Escherichia coli and purified to homogeneity. The activity of the C23O required the reduced form of the Fe(II) ion since the enzyme was highly susceptible to inactivation with hydrogen perocide but reactivated with the addition of ferrous sulfate in conjunction with ascorbic acid. The C23O activity was abolished by treatment with the chemical reagents, diethyl-pyrocarbonate (DEPC), tetranitromethane (TNM), and 1-cyclohexy1-3-(2-morpholinoethyl) car-bodiimidemetho-ρ-toluenesulfontate (CMC), which are modifying reagents of histidine, tyrosine and glutamic acid, respectively. These results suggest that histidine, tyrosine and glutamic acid residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues among several extradion dioxygenases and have the chemical potential to serveas ligands for Fe(II) coordination. Analysis of random point mutants in the C23O gene derived by PCR technique revealed that the mutated positions of two mutants, T179S and S211R, were located near the conserved His165 amd Hos217 residues, respectively. This finding indicates that these two positions, along with the conserved histidine residues, are specially effective regions for the enzyme function.