Purification, crystallization and properties of triacylglycerol lipase from Pseudomonas fluorescens

Sugiura, Masahiro; Oikawa, Tsutomu; Hirano, Kazuyuki; Inukai, Tadahiko

doi:10.1016/0005-2760(77)90194-1

Cited by 85 publications

(30 citation statements)

References 19 publications

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“…fluorescens. 19 ) Cationic surfactants such as cetyltrimethylammonium bromide tended to reduce the lipolytic activity of the purified enzyme. On the oth,er hand, the activity of the crude enzyme preparation was rather inhibited by anionic surfactants as reported previously.…”

Section: Discussionmentioning

confidence: 99%

Purification and Some Properties of Lipase Produced byPseudomonas fragi22.39 B

Nishio

Chikano

Kamimura

1987

Agricultural and Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Purification and Some Properties of Lipase Produced byPseudomonas fragi22.39 B

Nishio

Chikano

Kamimura

1987

Agricultural and Biological Chemistry

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“…The colipase preparation was a mixture of colipase 1 and 2. Lipase from Pseudomonas fluorescens (24) was a kind gift from Amano Pharmaceutical Co. (Nagoya, Japan).…”

Section: Introductionmentioning

confidence: 99%

Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts.

Bläckberg¹,

Hernell²,

Bengtsson³

et al. 1979

J. Clin. Invest.

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“…was produced by Sugihara (1991) in culture medium containing 1% olive oil 22 . It was reported that palm oil was the best substrate for the production of the extracellular lipase of Rhodotorula glutinis 23 . Marigold oil is a volatile oil and this oil has negative effect on cell growth.…”

Section: Effect Of Carbon Source In the Culture Mediummentioning

confidence: 99%

Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2

Ozgen

Attar

Elalmış

et al. 2016

Polish Journal of Chemical Technology

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A strain of Haloarcula hispanica isolated from Tuzkoy salt mine, Turkey exhibited extracellular lipolytic activity. Important parameters such as carbon sources and salt concentration for lipase production were investigated. Optimal conditions for the enzyme production from Haloarcula hispanica 2TK2 were determined. It was observed that the lipolytic activity of Haloarcula hispanica was stimulated by some of the carbon sources. The high lipase acitivity values were obtained in the presence of 2% (v/v) walnut oil (6.16 U/ml), 1% (v/v) fi sh oil (5.07 U/ml), 1% (v/v) olive oil (4.52 U/ml) and 1% (w/v) stearic acid (4.88 U/ml) at 4M NaCl concentration. Lipase was partially purifi ed by ammonium sulfate precipitation and ultrafi ltration. Optimal temperature and pH values were determined as 45 o C and 8.0, respectively. Lipase activity decreased with the increasing salt concentration, but 85% activity of the enzyme was maintained at 5M NaCl concentration. The enzyme preserved 41% of its relative activity at 90 o C. The partially purifi ed lipase maintained its activity in the presence of surfactants such as Triton X-100 and SDS. Therefore, the lipase which is an extremozyme may have potential applications especially in detergent industry.

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Purification, crystallization and properties of triacylglycerol lipase from Pseudomonas fluorescens

Cited by 85 publications

References 19 publications

Purification and Some Properties of Lipase Produced byPseudomonas fragi22.39 B

Purification and Some Properties of Lipase Produced byPseudomonas fragi22.39 B

Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts.

Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2

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