Factors Governing the Activity of Lyophilised and Immobilised Lipase Preparations in Organic Solvents

Persson, Mattias; Wehtje, Ernst; Adlercreutz, Patrick

doi:10.1002/1439-7633(20020603)3:6<566::aid-cbic566>3.0.co;2-7

Cited by 59 publications

(29 citation statements)

References 37 publications

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“…Several methods to overcome this disadvantage have been investigated. Reversed micelles [10], the immobilization on a variety of materials [11], or surface modification of the enzyme can be employed [12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Activation of subtilisin Carlsberg in hexane by lyophilization in the presence of fumed silica

Würges

Pfromm

Rezac³

et al. 2005

Journal of Molecular Catalysis B: Enzymatic

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Subtilisin Carlsberg (SC) was lyophilized from an aqueous buffer solution containing different amounts of unmodified commercial fumed silica. The activity of the enzyme/fumed silica preparation in hexane was compared to pure freeze-dried enzyme, and to a freeze-dried preparation reported in the literature with potassium chloride as additive. A sharp increase in enzyme activity was found to correlate with an increasing amount of fumed silica added to the enzyme solution prior to freeze-drying. A weight-ratio of 98.5wt% fumed silica relative to the mass of the final enzyme/fumed silica preparation led to about 130 fold increased activity of SC in hexane (when compared to pure lyophilized SC in hexane). This is about twice the activation effect compared to including potassium chloride in the buffer solution before freeze-drying [1].When freezing at -20ºC instead of in liquid nitrogen, even better activation was observed with fumed silica. We hypothesize that the activation of SC in hexane by immobilization of the enzyme on fumed silica is likely due to the distribution of the enzyme on the large surface area of fumed silica. This alleviates mass transfer limitations.

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Section: Introductionmentioning

confidence: 99%

Activation of subtilisin Carlsberg in hexane by lyophilization in the presence of fumed silica

Würges

Pfromm

Rezac³

et al. 2005

Journal of Molecular Catalysis B: Enzymatic

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“…Several physical and chemical methods such as chemical modification [215], immobilization [216], protein engineering [217] and directed evolution [218] have been employed for obtaining enzymes stable in the presence of organic solvents [219,220]. However, if enzymes are naturally stable and exhibit high activities in the presence of organic solvents, the stabilization of enzymes will not be required.…”

Section: Alkaline Proteases From Organic Solvent Tolerant Microbesmentioning

confidence: 99%

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Garg¹,

Singh²

2015

Enz Eng

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Since the advent and release of Bio 40 (the first detergent with bacterial alkaline protease) in 1959, exploration of the microbial alkaline proteases has been exploited beyond expectations. The inventory of microbial alkaline proteases is difficult to draft as it is increasing daily. Most of these proteases are the result of studies in which one or a few isolates were targeted for an alkali-stable enzyme. Although, the worldwide research on microbial alkaline proteases has been widely performed, we still need an improved enzyme capable of catalyzing reactions under extreme conditions (also called as extremozymes), e.g., high alkalinity and salinity, anhydrous environment, cold and hot environment, etc. As the search for extremozymes is in progress, it is imperative to explore the extreme environments to get some novel microbial strains (extremophiles) for alkali-stable proteases. This review article is an effort to compile the scattered information on some extremophiles and their alkali-stable proteases, which may have better specific industrial applications. It includes: (i) various extreme environments relevant to industrial biocatalysts, (ii) strategies of extremophilic microbes and enzymes which make them able to tolerate such conditions, and (iii) an overview of some important work done so far to explore industrially relevant extremophilic enzymes from extremophiles.

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“…Nevertheless, the influence of water on biocatalysis, remains unclear and needs to be further elucidated. In particular, no general trend has been found for the dependence of selectivity, especially enantioselectivity, on a W [6,7].…”

Section: Introductionmentioning

confidence: 95%

Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography

Márton

Chaput

Pierre

et al. 2010

Biotechnology Journal

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Fax : +33 5 46 45 82 65Abbreviations: IGC, Inverse Gas Chromatography a W , water thermodynamic activity, CALB, Candida antarctica Lipase B, BET, Brunauer-Emmet-Teller. AbstractThe adsorption of water and substrate on immobilized Candida antarctica lipase B was studied by performing adsorption isotherm measurements and using Inverse Gas Chromatography (IGC). Water adsorption isotherm of the immobilized enzyme showed singular profile absorption incompatible with the BET model, probably due to the hydrophobic nature of the support, leading to very low interactions with water. IGC allowed determining the evolution with a W of both dispersive surface energies and acidity and basicity constants of immobilized enzyme. These results showed that water molecules progressively covered immobilized enzyme, when increasing a W , leading to a saturation of polar groups above a W 0.1 and full coverage of the surface above a W 0.25. IGC also enabled relevant experiments to be performed to investigate the behavior of substrates under a W that they will experience, in a competitive situation with water. Results indicated that substrates had to displace water molecules in order to adsorb on the enzyme from a W values between 0.1 to 0.2, depending on the substrate. As the conditions used for these adsorption studies resemble the ones of the continuous enzymatic solid/gas reactor, in which activity and selectivity of the lipase were extensively studied, it was possible to link adsorption results with particular effects of water on enzyme properties.

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Factors Governing the Activity of Lyophilised and Immobilised Lipase Preparations in Organic Solvents

Cited by 59 publications

References 37 publications

Activation of subtilisin Carlsberg in hexane by lyophilization in the presence of fumed silica

Activation of subtilisin Carlsberg in hexane by lyophilization in the presence of fumed silica

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Lipase hydration state in the gas phase: Sorption isotherm measurements and inverse gas chromatography

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