amino acod

In order to evaluate microbial community structure dominated metabolic function profiles in large-scale food waste (FW) biotreatment systems, bacterial, archaeal and fungal community associated with metabolic function in high-temperature aerobic fermentation (AF) and anaerobic co-digestion (AcoD) processes were comprehensively investigated in this study. The qPCR results showed the higher gene copies of bacteria and fungi in initial and AF-treated FW compared with AcoD-treated FW, as well as bacteria and archaea in AcoD-treated FW were highly abundant among detected samples...

This study investigated volatile and nonvolatile metabolite profiles of makgeolli (a traditional rice wine in Korea) fermented by koji inoculated with Saccharomycopsis fibuligera and/or Aspergillus oryzae. The enzyme activities in koji were also examined to determine their effects on the formation of metabolites. The contents of all 18 amino acids detected were the highest in makgeolli fermented by S. fibuligera CN2601-09, and increased after combining with A. oryzae CN1102-08, unlike the contents of most fatty acids...

Ozonation of 11 naphthalene sulfonic acids (NSA) in the aqueous solution was studied by bubbling at 31 degrees C at an ozone dose rate of 5.56 mg min(-1) l(-1). COD, TOC and BOD5 of these compounds were tested. It was found that COD and TOC can be removed effectively by ozonation as expected. More than 40% COD of compounds No. I (2-amino-1-NSA), No. 5 (1-hydroxy-7-amino-5-NSA), No. 6 (6-hydroxy-1-NSA), No. 8 (6-amino-1,4-naphthalene disulfonic acid) and No. 11 (I -hydroxy-6-amino-3-NSA) has been eliminated at an ozone dosage of 5...

The degradation of 1,2-dichloroethane (DCE) by Xanthobacter autotrophicus GJ10 proceeds via chloroacetaldehyde (CAA), a toxic intermediate in the cells if it is not metabolized further by the NAD(+)-dependent CAA dehydrogenases. Here, we describe the cloning, sequence and expression in Escherichia coli of aldA, a plasmid-located CAA dehydrogenase-encoding gene of GJ10 as well as a chromosomal homolog, designated aldB. The DNA-predicted amino acid (aa) sequences of the two proteins (505 aa in AldA and 506 aa in AldB) are 84% identical...

The acoD gene, which encodes a dihydrolipoamide dehydrogenase component of the acetoin dehydrogenase enzyme system of Klebsiella pneumoniae was isolated and the nucleotide sequence determined. The gene is capable of encoding a protein of 465 amino acid residues with conserved binding domains for NAD and FAD, and two redox-active cysteine residues. The acoD gene product exhibited a Michaelis constant of 170 microM for NAD, while NADP can not be used as a substrate. The purified enzyme appeared to be a dimer of the acoD gene product...

Escherichia coli aldB was identified as a gene that is negatively regulated by Fis but positively regulated by RpoS. The complete DNA sequence determined in this study indicates that aldB encodes a 56.3-kDa protein which shares a high degree of homology with an acetaldehyde dehydrogenase encoded by acoD of Alcaligenes eutrophus and an aldehyde dehydrogenase encoded by aldA of Vibrio cholerae and significant homology with a group of other aldehyde dehydrogenases from prokaryotes and eukaryotes. Expression of aldB is maximally induced during the transition from exponential phase to stationary phase...

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The N-terminal amino acid sequence of purified acetaldehyde dehydrogenase II (AcDH-II) from ethanol-grown cells of Alcaligenes eutrophus was determined. By using oligonucleotides deduced from this sequence the structural gene for AcDH-II, which was referred to as acoD, was localized on a 7.2-kbp EcoRI restriction fragment (fragment D), which has been cloned recently (C. Fründ, H. Priefert, A. Steinbüchel, and H. G. Schlegel, J. Bacteriol. 171:6539-6548, 1989). A 2.8-kbp PstI subfragment of D, which harbored acoD, was sequenced...