Journal of Microbiology

Research Support, Non-U.S. Gov't

Characterization of an Extracellular Lipase in Burkholderia sp. HY-10 Isolated from a Longicorn Beetle: Doo-Sang Park , Hyun-Woo Oh , Sun-Yeon Heo , Woo-Jin Jeong , Dong Ha Shin , Kyung Sook Bae , Ho-Young Park; J. Microbiol. 2007;45(5):409-417.; DOI: https://doi.org/2596 [pii]

Abstract: Burkholderia sp. HY-10 isolated from the digestive tracts of the longicorn beetle, Prionus insularis, produced an extracellular lipase with a molecular weight of 33.5 kDa estimated by SDS-PAGE. The lipase was purified from the culture supernatant to near electrophoretic homogenity by a one-step adsorption-desorption procedure using a polypropylene matrix followed by a concentration step. The purified lipase exhibited highest activities at pH 8.5 and 60°C. A broad range of lipase substrates, from C4 to C18 ρ-nitrophenyl esters, were hydrolyzed efficiently by the lipase. The most efficient substrate was ρ-nitrophenyl caproate (C6). A 2485 bp DNA fragment was isolated by PCR amplification and chromosomal walking which encoded two polypeptides of 364 and 346 amino acids, identified as a lipase and a lipase foldase, respectively. The N-terminal amino acid sequence of the purified lipase and nucleotide sequence analysis predicted that the precursor lipase was proteolytically modified through the secretion step and produced a catalytically active 33.5 kDa protein. The deduced amino acid sequence for the lipase shared extensive similarity with those of the lipase family I.2 of lipases from other bacteria. The deduced amino acid sequence contained two Cystein residues forming a disulfide bond in the molecule and three, well-conserved amino acid residues, Ser131, His330, and Asp308, which composed the catalytic triad of the enzyme.

Isolation and characterization of 4-chlorophenoxyacetic acid-degrading bacteria from agricultural soils: Chung, Min Jae , Shin, Se Young , Park, Yong Keun , Min, Kyung Hee , Ka, Jong Ok; J. Microbiol. 1997;35(2):117-122.

Abstract: Several dominant 4-CPA-degrading bacteria were isoalted from agricultural soils. Most of the isolates were identified as Burkholderia species by fatty acid methyl ester (FAME) analysis, but they were distinct in chromosomal patterns obtained by PCR amplification of repetitive extragenic palindromic (REP) sequences. These strains were generally restricted in their substrate utilization capabilities. The 4-CPA degradative enzymes were idnducible by 4-CPA and some isolates appeared to mineralize 4-CPA via formation of 4-chlorophenol and 4-chlorocatechol as intermediates during its biodegradation pathway. Plasmid DNAs were not detected from most of the isolates and their 4-CPA genes wer on the chromosomal DAN. The 4-CPA degradation patterns in axenic cultures and natural soils varied depending on the strains and soils. The inoculation of 4-CPA degraders much improved the removal of 4-CPA from the 4-CPA treated soils.

Identification and Characterization of Aniline-Degrading Bacteria Isolated from Soil and Wastewater: Shin, Se Young , Chung, Min Jae , Yi, Haak Rho , Kim, Chi Kyung , Min, Kyung Hee , Ka, Jong Ok; J. Microbiol. 1998;36(2):80-85.

Abstract: Twenty two aniline-degrading bacteria were isolated from agricultural soil and wastewater. The isolates were able to utilize aniline as the sole source of carbon and nitrogen. A total of 45% of the isolates were identified to the species level by fatty acid methyl ester (FAME) analysis; the isolates were found to be strains of the Burkholderia, Nocardia, Arthrobacter, and Rhodococcus species. Their chromosomal patterns, obtained by polymerase chain reaction (PCR) amplification of repetitive extrogenic palindromic(REP) sequences, were distinct from each other. Plasmid DNAs were detected from 45% of the isolates, but only one strain, ANL5, was shown to have a transmissible, aniline degradative plasmid. The isolates were very restricted in their substrate utilization abilities. Aniline degradative enzymes were inducible by the presence of aniline, and most of the isolates appeared to mineralize aniline through an ortho-cleavage path-way using catechol 1,2-dioxygenase.

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