Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading bacterium Acinetobacter calcoaceticus RAG-1

Reddy, P. Jayarama; Allon, R.; Mevarech, Moshe; Mendelovitz, Simona; Sato, Yoshiaki; Gutnick, David L.

doi:10.1016/0378-1119(89)90016-4

Cited by 42 publications

(23 citation statements)

References 27 publications

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“…The prois identical to the Gly-XI-Ser-X,-Gly box found in lipases gram ' Terminator' identified this sequence (or part of it) and esterases, as well as in serine proteinases (Brenner, as a possible rho-independent terminator for trans-1988; Boel et al, 1988). The serine in this sequence is cription (Rosenberg & Court, 1979), starting from the (Feller et al, 1991), P23872 is the E. coli hypothetical protein (Miyamoto et al, 1991), P15304 is the rat lipase (Holm et al, 1988) and P18773 is the esterase of A. calcoaceticus RAG-1 (Reddy et al, 1989). Homology is indicated above the amino acid sequences; asterisks denote amino acids perfectly conserved in all five proteins and dots denote well-conserved amino acids.…”

Section: R G Kok and Othersmentioning

confidence: 99%

Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases

Kok¹,

Christoffels²,

Vosman³

et al. 1993

Journal of General Microbiology

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Acinetobacter calcoaceticus BD413, when grown in batch culture in nutrient broth, produces both extracellular lipase activity and cell-bound esterase activity during and after the transition between exponential growth and the stationary phase. From a library of A. calcoaceticus DNA in Escherichia cofi, plasmids were isolated that enabled E. coli to grow on media with tributyrin as the sole carbon source. Assays with model substrates classified the product of the cloned gene as an esterase. Via deletion analysis, the esterase gene was mapped on a 1.8 kbp chromosomal DNA fragment. This fragment was sequenced and found to contain one open reading frame, termed estA, which encodes a protein of 40.0 kDa. The amino acid sequence of this protein shows homology to a number of lipolytic enzymes, most notably to esterases. Deletion of estA only partially abolished cell-bound esterase activity in A. calcoaceticus, indicating that BD413 forms at least two esterases. Both esterases show the same temporal regulation of expression. /?-Galactosidase activity was measured in strains in which a promoterless lac2 gene was inserted into estA. Induction of lac2 expression in these strains also occurred at the end of exponential growth in batch cultures, indicating that production of the esterase is regulated at the genetic level.

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Section: R G Kok and Othersmentioning

confidence: 99%

Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases

Kok¹,

Christoffels²,

Vosman³

et al. 1993

Journal of General Microbiology

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“…Acknowledging the advantages and applications of biosurfactantesterase complex, the correlation in their production during the growth of microbes seemed to have caught attention of many researchers [3,14,[44][45][46][47][48]. Studies undertaken on biosurfactant-esterase complex are given in chronological order in table 5.…”

Section: Correlation Between Biosurfactant Production and Esterase Acmentioning

confidence: 99%

“…Results emphasized that the capability of producing emulsan facilitated the cells to grow on crude oil. Furthermore, a putative esterase gene (est) from A. calcoaceticus RAG-1 was cloned into Escherichia coli [47]. Esterasepositive clones exhibited high levels of esterase activity even in intact cells.…”

Section: Correlation Between Biosurfactant Production and Esterase Acmentioning

confidence: 99%

Biosurfactant Production and Potential Correlation with Esterase Activity

Sekhon¹

2012

J Pet Environ Biotechnol

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Biosurfactants (microbial surfactants) are surface active compounds produced extracellularly or as part of the cell membrane by several bacterial and fungal species. They have the unique property of reducing the surface and interfacial tension of liquids. Biosurfactants have applications in the field of agriculture, petroleum, microbial enhanced oil recovery, biomedical sciences, cosmetics, food processing and pharmaceuticals. The global biosurfactants market has grown gradually. Regardless of their greater biodegradability and reduced toxicity, cost competitiveness still remains the major concern for biosurfactant production. However, recombinant or metabolically engineered hyper producing strains combined with optimized cultivation conditions have made it possible for many companies to reap the benefits of 'green' biosurfactant technology. Simultaneously, biosurfactants and bioemulsifiers showing esterase activities and having potential applications are reported to form stable oil-water emulsions with hydrophobic substrates such as hexadecane and polyaromatic hydrocarbons. Biosurfactant production and release of esterases by the microbial cells is shown to be synchronized and symbiotically beneficial in some species. Several bacterial biosurfactant and esterase genes have been identified, cloned and expressed for their enhanced production. This

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“…Strain RAG-1 isolated from Israeli sea water near a beach was originally described as Arthrobacter RAG-1. It was later referred to as A. calcoaceticus RAG-1 Gutnick, 1985, 1986;Minas et al, 1988;Reddy et al, 1989;Leahy et al, 1993;Zhang et al, 1997;Sullivan et al, 1999;Johri et al, 2002) or A. lwoffii RAG-1 (Alon and Gutnick, 1993; Gutnick, 2001, 2003), A. junii (Menezes et al, 2005), and A. radioresistens (Pessione et al, 1996(Pessione et al, , 2003Pessione and Giunta, 1997). In parallel, Acinetobacter venetianus strain VE-C3 was isolated from a Venice lagoon and described by Di Cello et al (1997).…”

mentioning

confidence: 99%

Safety Assessment of Transgenic Organisms, Volume 4

2010

Harmonisation of Regulatory Oversight in Biotechnology

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Cloning and expression in Escherichia coli of an esterase-coding gene from the oil-degrading bacterium Acinetobacter calcoaceticus RAG-1

Cited by 42 publications

References 27 publications

Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases

Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases

Biosurfactant Production and Potential Correlation with Esterase Activity

Safety Assessment of Transgenic Organisms, Volume 4

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