Crystallization and Preliminary X-ray Studies of Lipase B from Candida antarctica

Uppenberg, J.; Patkar, Shamkant; Bergfors, Terese; Jones, T. Alwyn

doi:10.1006/jmbi.1994.1035

Cited by 112 publications

(54 citation statements)

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“…The other advantages include reduced environmental load of detergent products, reduced use of chemicals in detergents, biodegradable, no negative impact on disposal of domestic waste and no risk for aquatic organisms. Recombinant cold active lipase from C. antarctica is successfully used in detergent formulation (Uppenberg et al 1994b). CLPs from Microbacterium phyllosphaerae and B. sphaericus were reported to be efficient in the removal of lipid stains in the presence of commercial detergents from fabrics (Joseph & Ramteke 2013).…”

Section: Applications In the Detergent Industrymentioning

confidence: 99%

Cold active lipases – an update

Kavitha

2016

Frontiers in Life Science

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Cold active lipases (CLPs) are gaining importance nowadays as they are increasingly used in fine chemical synthesis, bioremediation, food processing and as detergent additive. These enzymes exhibit high catalytic activity at low temperatures and flexibility to act at low water medium. Since they are active at low temperatures consume less energy and also stabilize fragile compounds in the reaction medium. CLPs are commonly obtained from psychrophilic microorganisms which thrive in cold habitats. Compared to mesophilic and thermophilic lipases, only a few CLPs were studied and industrially exploited so far. CLPs (C. antarctica lipase-A and C. antarctica lipase-B) from Candida antarctica isolated from Antarctic region are the well studied and industrially employed, and many are being followed up. This review updates the CLPs reported recently and the industrial applications of CLPs. ARTICLE HISTORY

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Section: Applications In the Detergent Industrymentioning

confidence: 99%

Cold active lipases – an update

Kavitha

2016

Frontiers in Life Science

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“…This immobilized preparation is obtained by the immobilization of lipase B from Candida antarctica via the interfacial activation of the enzyme on a moderately hydrophobic resin, Lewatit VP OC 1600 (Uppenberg et al, 1994).…”

Section: Interesterifi Cation Of Egg-yolk Pc With Linseed Oilmentioning

confidence: 99%

Lipase-catalyzed interesterification of egg-yolk phosphatidylcholine and plant oils

Chojnacka¹,

Gładkowski²,

Kiełbowicz³

et al. 2014

Grasas y Aceites

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SUMMARY:The incorporation of polyunsaturated fatty acids into the sn-1 position of egg-yolk phosphatidylcholine (PC) in the process of lipase-catalyzed interesterification was investigated. For this purpose plant oils containing these acids in the triacylglycerol (TAG) form were used as acyl donors and three commercially available immobilized lipases were examined as biocatalysts. In all the experiments the best results were obtained using Novozym 435. After 72 h of the reaction of PC with linseed oil the maximum incorporation of α-linolenic acid into PC was 34%. The result of this reaction was also a reduction in the n-6/n-3 ratio in egg-yolk PC from 24.5 to 0.7. The highest incorporation n-6 PUFAs into PC were obtained with evening primrose oil as the acyl donor, and in this case, 50.7% of n-6 PUFA as the sum of linoleic and γ-linolenic was achieved. The highest content of γ-linolenic acid in modified PC (7.3%) was achieved in the reaction of PC with borage oil. KEYWORDS:Egg-yolk phosphatidylcholine; Interesterification; Lipase; Plant oil; Polyunsaturated fatty acids; Structured phospholipids RESUMEN: Interesterificación de fosfatidilcolina de yema de huevo y aceites vegetales catalizada por lipasas. Se ha investigado la incorporación de ácidos grasos poliinsaturados en la posición sn-1 de fosfatidilcolina de yema de huevo (PC) en el proceso de interesterificación catalizado por lipasas. Para lograr este propósito, fueron examinados aceites vegetales que contienen estos ácidos en la forma de triacilgliceroles (TAG) como donadores de acilo y tres lipasas inmovilizadas disponibles comercialmente. En todos los experimentos los mejores resultados se obtuvieron para Novozym 435. La incorporación máxima de ácido α-linolénico en PC fue del 34% después de 72h de la reacción de PC con aceite de linaza. El resultado de esta reacción fue también la reducción de la relación de n-6/n-3 en PC de yema de huevo de 24.5 a 0.7. La incorporación más alta de n-6 PUFAs en PC se logró para el aceite de onagra como donador de acilo, en este caso se alcanzó el 50.7% de n-6 PUFA, como suma de los ácidos linoleico y γ-linolénico. El mayor contenido de ácido γ-linolénico en PC modificado (7.3%) se logró en la reacción de PC con aceite de borraja.

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“…This is called the closed form of lipases., in In certain cases the active center is not fully secluded from the medium (e.g. lipase B from Candida antarctica) (Uppenberg et al, 1994), whereas in other cases the lid fully blocks the active center (e,g, lipases from Thermomyces lanuginosus (Brady et al, 1990) or Rhizomur miehei (Derewenda et al, 1992)), while in a few cases the enzyme even has a double lid that moves in a coordinated form (e.g., lipase from Bacillus thermocatenulatus) (Carrasco-López et al, 2009). This closed form is in equilibrium with an open form where this lid is displaced exposing a very large hydrophobic pocket to the medium (Brzozowski et al, 1991, Van Tilbeurgh et al, 1993.…”

Section: 1-the Case Of Lipases Immobilization Via Interfacial Activmentioning

confidence: 99%

Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

Barbosa

Ortíz

Berenguer-Murcia

et al. 2015

Biotechnology Advances

596

318

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Enzyme immobilization and purification are two steps that are usually required in the development of any industrial biocatalyst. In this review, we detail the efforts performed to couple the purification and the immobilization of industrial enzymes in a single step. The use of antibodies (versus the target enzyme or versus some domains), the development of specific domains with affinity for some specific supports or just to increase the affinity for standard ones (ionic exchangers, silicates) will be revised. We will show how the control of the immobilization conditions may convert some unspecific supports in largely specific ones. The development of tailormade heterofunctional supports as a tool to immobilize-stabilize-purify some proteins will be discussed in deep, using low concentration of adsorbents groups and a dense layer of groups able to give an intense multipoint covalent attachment. The final coupling of mutagenesis and tailor made supports will be a the last part of the review.

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Crystallization and Preliminary X-ray Studies of Lipase B from Candida antarctica

Cited by 112 publications

References 0 publications

Cold active lipases – an update

Cold active lipases – an update

Lipase-catalyzed interesterification of egg-yolk phosphatidylcholine and plant oils

Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

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