Purification and partial characterization of an alkaline lipase from Pseudomonas pseudoalcaligenes F-111

Lin, Shuen-Fuh; Chiou, Chien-Ming; Yeh, Chuan-Mei; Tsai, Ying-Chieh

doi:10.1128/aem.62.3.1093-1095.1996

Cited by 67 publications

(17 citation statements)

References 14 publications

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“…zymograms. Other investigators have also reported aggregation of purified lipases to a varying degree [21,[26][27][28]. Application of purified LipA to wells in Spirit Blue agar indicator plates containing an emulsion of tributyrin also indicates activity toward this lipidic substrate (not shown).…”

Section: R E S U L T S a N D Discussionmentioning

confidence: 89%

Purification and properties of the extracellular lipase, LipA, of Acinetobacter sp. RAG‐1

Snellman

Sullivan

Colwell

2002

European Journal of Biochemistry

133

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An extracellular lipase, LipA, extracted from Acinetobacter sp. RAG-1 grown on hexadecane was purified and properties of the enzyme investigated. The enzyme is released into the growth medium during the transition to stationary phase. The lipase was harvested from cells grown to stationary phase, and purified with 22% yield and > 10-fold purification. The protein demonstrates little affinity for anion exchange resins, with contaminating proteins removed by passing crude supernatants over a Mono Q column. The lipase was bound to a butyl Sepharose column and eluted in a Triton X-100 gradient. The molecular mass (33 kDa) was determined employing SDS/PAGE. LipA was found to be stable at pH 5.8-9.0, with optimal activity at 9.0. The lipase remained active at temperatures up to 70°C, with maximal activity observed at 55°C. LipA is active against a wide range of fatty acid esters of p-nitrophenyl, but preferentially attacks medium length acyl chains (C 6 , C 8 , but shows no loss in activity after incubation with other metals or inhibitors examined in this study. The protein retains more than 75% of its initial activity after exposure to organic solvents, but is rapidly deactivated by pyridine. RAG-1 lipase offers potential for use as a biocatalyst.

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Section: R E S U L T S a N D Discussionmentioning

confidence: 89%

Purification and properties of the extracellular lipase, LipA, of Acinetobacter sp. RAG‐1

Snellman

Sullivan

Colwell

2002

European Journal of Biochemistry

133

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“…2 b). LIN et al (1996) and SHARON et al (1998) reported temperature optima of 40 °C and 45 °C for P. pseudoalcaligenes and P. aeruginosa KKA-5, respectively. On the other hand, KOJIMA et al (1994) reported a lipase from P. fluorescens AK-102 with temperature optima of 55 °C and thermostability below 50 °C.…”

Section: Resultsmentioning

confidence: 99%

“…They hydrolyse fats into fatty acids and glycerol at the water-lipid interface and can reverse the reaction in non-aqueous medium ( JAEGER et al 1999). Several alkaline and thermostable lipases exhibiting high activities have been characterized from microorganisms, namely Pseudomonas pseudoalcaligenes (LIN et al 1996), P. fragi (SCHUEPP et al 1997) and P. aeruginosa (SHARON et al 1998). There is an increasing demand for specific lipases ( JAEGER et al 1999).…”

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confidence: 99%

Properties of a thermostable and solvent stable extracellular lipase from aPseudomonas sp. AG-8

Sharma

Tiwari

Hoondal

2001

J. Basic Microbiol.

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An extracellular lipase isolated from Pseudomonas sp. AG‐8, had an optimal activity at 45 °C and pH 8.0–8.5. It retained more than 80% of its initial activity after keeping for 1 h at 65 °C. The enzyme was stable in 5 M NaCl and 6 M urea. Triton X‐100 increased the lipase activity by 2.4 fold. Ca2+ ions activated the enzyme, while Zn2+, Fe2+, Fe3+ strongly inhibited its activity. Ethanol, methanol and acetone at 20% (v/v) enhanced the lipase activity by 2.9, 3.6 and 4.5 fold respectively. Dimethylsulphoxide at 90% (v/v) enhanced the enzyme activity up to 5.7 fold.

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“…The optimum temperature value is similar to values previously reported for other Pseudomonas sp. lipases [34,35]. The high activity of the ES3 lipase at relatively low temperatures and high pH values suggests that its incorporation into detergent formulations would provide economic benefits to the industry.…”

Section: Effects Of Ph and Temperature On Lipase Activitymentioning

confidence: 99%

The Use of Boron Compounds for Stabilization of Lipase from Pseudomonas aeruginosa ES3 for the Detergent Industry

Saraç

Uğur

Boran

et al. 2015

J Surfact & Detergents

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This study aimed to characterize a lipase that is highly active and stable under typical washing conditions for use as a detergent ingredient by investigating the effects of various boron compounds on lipase stabilization under different conditions. In addition, the antimicrobial activity of the boron compounds used in enzyme stabilization was examined in order to obtain an effective antimicrobial detergent. A lipase-producing bacterium was isolated from kitchen wastewater samples using Rhodamine-B Agar medium and identified as Pseudomonas aeruginosa based on 16S rDNA sequence analysis. The ES3 lipase obtained from P. aeruginosa was purified, and the purified enzyme was found to have a molecular mass of 40 kDa. The enzyme showed optimal activity at pH 9.0-10.0 and 40°C and remained stable in the presence of various metal ions, surfactants and oxidizing agents. Moreover, the pH stability and thermostability of the enzyme was improved by the addition of boron compounds, which, when used as stabilizers in the incubation media, also increased the stability of the enzyme towards commercial detergents. Furthermore, the enzyme displayed properties comparable with the commercial product Lipolase Ò , which has shown excellent stability towards various commercial detergents. Finally, boron compounds used to stabilize the lipase were found to possess antimicrobial properties, suggesting that detergents incorporating these compounds will also exhibit antimicrobial activity when washing clothes and dishes. , Turkey since 2003. Her main research areas are structural biology and biomolecular NMR spectroscopy. Her current research focuses on structure-dynamics relationships in ubiquitin-like modification systems. J Surfact Deterg (2015) 18:275-285 285

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Purification and partial characterization of an alkaline lipase from Pseudomonas pseudoalcaligenes F-111

Cited by 67 publications

References 14 publications

Purification and properties of the extracellular lipase, LipA, of Acinetobacter sp. RAG‐1

Purification and properties of the extracellular lipase, LipA, of Acinetobacter sp. RAG‐1

Properties of a thermostable and solvent stable extracellular lipase from aPseudomonas sp. AG-8

The Use of Boron Compounds for Stabilization of Lipase from Pseudomonas aeruginosa ES3 for the Detergent Industry

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