Cloning, Nucleotide Sequencing, and Expression in Escherichia coli of a Lipase and Its Activator Genes from Pseudomonas sp. KWI-56.

Iizumi, Taro; Nakamura, Kōichi; Shimada, Yuji; Sugihara, Akio; Tominaga, Yoshio; Fukase, Tetsuro

doi:10.1271/bbb1961.55.2349

Cited by 50 publications

(30 citation statements)

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“…ORF D4225 shows 21.8% identity in a 326 aa overlap with triacylglycerase lipase from Pseudomonas sp. (Iizumi et al, 1991). ORF D4241 has 28.9% identity in a 363 aa overlap with E. coli deoxyribodipyrimidine photolyase (Dorrell et al, 1993).…”

Section: Resultsmentioning

confidence: 99%

Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV

Brandt

Ramlow²,

Otto³

et al. 1996

Yeast

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Section: Resultsmentioning

confidence: 99%

Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV

Brandt

Ramlow²,

Otto³

et al. 1996

Yeast

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“…Pseudomonas glumae was also found to be efficient in a system of washing model (Iizumi et al, 1991, Jorgesen et al, 1991. Span 80 was chosen for the following studies as it showed the highest percentage of oil removal in the presence of lipase.…”

Section: Resultsmentioning

confidence: 99%

Lipase from thermoalkalophilic Pseudomonas species as an additive in potential laundry detergent formulations

Khoo¹,

Ibrahim²

2009

MJM

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Lipase isolated from a thermoalkalophilic Pseudomonas species was used as additive to improve the degree of olive oil removal from cotton fabric in the presence of surfactants. The lipase used in this study was found to be more effective with non ionic surfactants as compared to ionic surfactants. In terms of stability, there was no decrease in activity found in the presence of Tween 85, Span 80 and Span 20. Lipase from Pseudomonas species was most active in the presence of Tween 85, Span 80 and Span 20. The application of lipase from Pseudomonas species as an additive in the formulation containing Span 80 has improved oil removal by 36% using the washing system consisting 5 U/mL lipase, at 70 °C for 20 min and 0.8% of Span 80 as surfactant. Considering that lipase from Pseudomonas species is stable in high pH and temperatures in the presence of various surfactants, therefore it is suitable to be incorporated as additives in potential detergent formulations.

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“…fluorescens SIK W1 [23], B52 [24], and Pseudomonas sp. LS107d2 [25] [13], and 109 [15]. Class III lipases share two features: (a) the precursor protein possesses a signal peptide and (b) the supplemental gene downstream of the lipase gene is essential to express lipase activity in E. coli.…”

Section: Discussionmentioning

confidence: 99%

Lipase from Pseudomonas aeruginosa

Oshima-Hirayama¹,

Yoshikawa²,

Nishioka³

et al. 1993

European Journal of Biochemistry

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The lipase gene from Pseudornonas aeruginosa TE3285 is followed by another gene, fipB. The lipase gene was expressed in Escherichia coli BL21(DE3)pLysS using the T7 RNA polymerase expression system. The mature lipase was accumulated as inclusion bodies at 42% of the total cell proteins. The inclusion bodies were solubilized with 8 M urea, but lipase activity was not detected in the solubilized preparation containing 85% lipase protein even after removing urea by dialysis. The lipB gene, positioned downstream of the lipase gene and thought to be necessary for the expression of the lipase gene, was expressed in Escherichia coli JM109 as a fusion with the glutathione transferase gene from Schisrosoma japonicurn. The fusion protein was partially purified on glutathione-agarose beads to 36% purity. Incubated with the fusion protein at a molar ratio of 1 : 1 at 4°C for 24 h, the solubilized lipase showed lipase activity of about a tenth that of the purified lipase prepared from Pseudornonas aeruginosa TE3285. Magnesium ions and ATP were not essential but increased the activation. When the fusion protein was treated with thrombin to release the glutathione transferase part, it retained its activity. The lipase activation with lipB protein probably proceeds to form a 1 : 1 complex with the inactive, solubilized lipase protein but by a different mode from known chaperones.

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Cloning, Nucleotide Sequencing, and Expression in Escherichia coli of a Lipase and Its Activator Genes from Pseudomonas sp. KWI-56.

Cited by 50 publications

References 0 publications

Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV

Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV

Lipase from thermoalkalophilic Pseudomonas species as an additive in potential laundry detergent formulations

Lipase from Pseudomonas aeruginosa

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