Effective Method for Activity Assay of Lipase from Chromobacterium viscosum1

Immobilized metal-ion affinity gel electrophoresis (IMAGE) has been demonstrated to be an efficient tool to study the binding of proteins to chelated transition metals such as Cu(II). IMAGE was exploited to isolate several lipases from different sources and so evaluate their affinities for iminodiacetic acid (IDA)-Cu(II) and, in particular, to evaluate their enzymatic activities while retained on a gel (IMAGE) containing chelated copper [IDA-Cu(II)]. It was found that all lipases can be active within the gel while being coordinated to IDA-Cu(II). It is concluded that active site histidine (most likely) is not involved in the metal recognition and thus other resident histidines serve as electron donors. This is mainly attributed to the known phenomenon of occlusion of the catalytic site by more or less rigid lid structures. The involvement of active site histidine in hydrogen bonding is also evoked.

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Copper binding studies of lipases from different sources using image binding: Mechanism of free copper and chelated copper

Colin

Vijayalakshmi

1996

J. Mol. Recognit.

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Continuous synthesis of glycerides by lipase in a microporous membrane bioreactor

Hoo

Yamané

Shimizu

et al. 1984

J Americ Oil Chem Soc

117

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A membrane bioreactor was developed for continuous synthesis of glycerides by lipase to overcome the drawbacks associated with the usual operation in an emulsion system. One unit (total area: 726 cm2) of flat, plate‐type dialyzer was used as the membrane bioreactor at 40 C. The glycerol solution, containing bacterial lipase and water, was supplied continuously to 1 side of a sheet of microporous polypropylene membrane (strongly hydrophobic) and the effluent was recycled, while undiluted liquid fatty acid (oleic or linoleic) was fed continuously to the opposite side of the membrane and came in contact with a glycerol‐water‐lipase solution to cause the reaction. The product, glycerides, was obtained at the outlet, in a pure state, with no other phase. Highest conversion (ca. 90%) was obtained when the water content of the glycerol solution was 3–4%. As the accumulation of water produced by the reaction lowered the conversion, molecular sieves in a column that the glycerol solution passed through were used for optimal water content. The reaction could be continued at least for 1 month, yielding a conversion above 70% when 1% CaCl2 was added in the glycerol solution. The main component of glycerides formed was almost equimolar amounts of mono‐and diglycerides.

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Hydrophobic interaction chromatography of Chromobacterium viscosum lipase

Queiroz

Garcı́a

1995

Journal of Chromatography A

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Effective Method for Activity Assay of Lipase from Chromobacterium viscosum1

Cited by 11 publications

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Copper binding studies of lipases from different sources using image binding: Mechanism of free copper and chelated copper

Copper binding studies of lipases from different sources using image binding: Mechanism of free copper and chelated copper

Continuous synthesis of glycerides by lipase in a microporous membrane bioreactor

Hydrophobic interaction chromatography of Chromobacterium viscosum lipase

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