Over-expression and properties of a purified recombinant Bacillus licheniformis lipase: a comparative report on Bacillus lipases

Nthangeni, Mulalo Bethuel; Patterton, Hugh-G.; Tonder, André van; Vergeer, Wilma P.; Litthauer, Derek

doi:10.1016/s0141-0229(01)00316-7

Cited by 93 publications

(80 citation statements)

References 26 publications

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“…The deduced amino acid sequence showed 45 to 50% sequence identity with mesophilic Bacillus family I-4 lipases (3,18,21,34), ϳ20% sequence identity with thermophilic Bacillus family I-5 lipases (2,11,29), but no identity with PHA depolymerase from P. lemoignei, except for the conserved pentapeptide (6). Functional expression and purification of the recombinant enzyme in E. coli.…”

Section: Resultsmentioning

confidence: 99%

Cloning and Sequencing of a Poly( dl -Lactic Acid) Depolymerase Gene from Paenibacillus amylolyticus Strain TB-13 and Its Functional Expression in Escherichia coli

Akutsu-Shigeno

Teeraphatpornchai

Teamtisong

et al. 2003

Appl Environ Microbiol

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The gene encoding a poly(DL-lactic acid) (PLA) depolymerase from Paenibacillus amylolyticus strain TB-13 was cloned and overexpressed in Escherichia coli. The purified recombinant PLA depolymerase, PlaA, exhibited degradation activities toward various biodegradable polyesters, such as poly(butylene succinate), poly(butylene succinate-co-adipate), poly(ethylene succinate), and poly(⑀-caprolactone), as well as PLA. The monomeric lactic acid was detected as the degradation product of PLA. The substrate specificity toward triglycerides and p-nitrophenyl esters indicated that PlaA is a type of lipase. The gene encoded 201 amino acid residues, including the conserved pentapeptide Ala-His-Ser-Met-Gly, present in the lipases of mesophilic Bacillus species. The identity of the amino acid sequence of PlaA with Bacillus lipases was no more than 45 to 50%, and some of its properties were different from those of these lipases.

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Section: Resultsmentioning

confidence: 99%

Cloning and Sequencing of a Poly( dl -Lactic Acid) Depolymerase Gene from Paenibacillus amylolyticus Strain TB-13 and Its Functional Expression in Escherichia coli

Akutsu-Shigeno

Teeraphatpornchai

Teamtisong

et al. 2003

Appl Environ Microbiol

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“…Additionally, the cloned lipase contains a His residue at position X 1 like other Bacillus lipases, while position X 2 is occupied by a Met, exclusive of subfamily I.4 [6]. The catalytic apparatus of lipases, involving the triad serine, glutamate or aspartate, and histidine [1] was located in the cloned protein, by similarity, at positions 78 (S), 134 (D), and 157 (H).…”

Section: Analysis Of the Lipase Coding Sequencementioning

confidence: 99%

“…Among lipase-producing bacteria, several Bacillus species have been shown to possess a lipolytic system well suited for biotechnological applications [1], and lipases from B. subtilis [3^4], B. pumilus [5], B. licheniformis [6], B. thermocatenulatus [7], B. thermoleovorans [8], or B. stearothermophilus [9] have already been described, puri¢ed or cloned. The increasing interest for bacterial lipases and new lipase-producing Bacillus strains led us to perform the analysis of Bacillus megaterium 370 lipolytic system.…”

Section: Introductionmentioning

confidence: 99%

Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I.4 bacterial lipase

Ruiz¹

2002

FEMS Microbiology Letters

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The lipolytic system of Bacillus megaterium 370 was investigated, showing the existence of at least two secreted lipases and a cell-bound esterase. A gene coding for an extracellular lipase was isolated and cloned in Escherichia coli. The cloned enzyme displayed high activity on short to medium chain length (C 4^C8 ) substrates, and poor activity on C 18 substrates. On the basis of amino acid sequence homology, the cloned lipase was classified into subfamily I.4 of bacterial lipases.

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“…The bottom phase was dialysed against ultra-pure water, lyophilised at a temperature of -50 °C and pressure of 1.2 x 10 -2 mbar for 48 h. The purified lipase showed activity of 175 U/g, pI of 3.12 and produced a single band on SDS-PAGE electrophoresis with an apparent molecular mass of approximately 54 kDa ( Figure 1S, supplementary material). According to Nthangeni et al, 24 lipases from generous Bacillus normally have a pI of between 6.3 and 9.4.…”

Section: Lipase Production and Purificationmentioning

confidence: 99%

Biochemical characterisation of lipase from a new strain of Bacillus sp. ITP-001

et al. 2012

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Recebido em 26/9/11; aceito em 24/1/12; publicado na web em 15/5/12Lipases are characterised mainly by catalytic versatility and application in different industrial segments. The aim of this study was to biochemically characterise a lipase from a new strain of Bacillus sp. ITP-001. The isoelectric point and molecular mass were 3.12 and 54 kDa, respectively. The optima lipase activity was 276 U g -1 at pH 7.0 and a temperature of 80 °C, showing greater stability at pH 5.0 and 37 °C. , respectively determined by the Eadie-Scatchard method.

show abstract

Over-expression and properties of a purified recombinant Bacillus licheniformis lipase: a comparative report on Bacillus lipases

Cited by 93 publications

References 26 publications

Cloning and Sequencing of a Poly( dl -Lactic Acid) Depolymerase Gene from Paenibacillus amylolyticus Strain TB-13 and Its Functional Expression in Escherichia coli

Cloning and Sequencing of a Poly( dl -Lactic Acid) Depolymerase Gene from Paenibacillus amylolyticus Strain TB-13 and Its Functional Expression in Escherichia coli

Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I.4 bacterial lipase

Biochemical characterisation of lipase from a new strain of Bacillus sp. ITP-001

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