Reaction rate with suspended lipase catalyst shows similar dependence on water activity in different organic solvents

Valivety, Rao H.; Halling, Peter J.; Macrae, Alasdair R.

doi:10.1016/0167-4838(92)90278-l

Cited by 276 publications

(134 citation statements)

References 10 publications

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“…[17][18][19][20] We tested nine organic solvents for capsinoid synthesis when catalyzed by Novozym 435 ( Table 2). The conversion yields reached equilibrium at 70.9-78.0z within 0.5 h with most of the solvents used except for hexane and chloroform.…”

Section: Choice Of Organic Solventmentioning

confidence: 99%

Enzymatic Synthesis of a Capsinoid by the Acylation of Vanillyl Alcohol with Fatty Acid Derivatives Catalyzed by Lipases

Kobata

Kawaguchi

Watanabe

2002

Bioscience, Biotechnology, and Biochemistry

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Section: Choice Of Organic Solventmentioning

confidence: 99%

Enzymatic Synthesis of a Capsinoid by the Acylation of Vanillyl Alcohol with Fatty Acid Derivatives Catalyzed by Lipases

Kobata

Kawaguchi

Watanabe

2002

Bioscience, Biotechnology, and Biochemistry

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“…The methodology for determining catalyst activity at known (pre-equilibrated) a, was as described previously (Valivety et al, 1992a). The rationale and reliability of this method was fully discussed there.…”

Section: Reactionsmentioning

confidence: 99%

Relationship between water activity and catalytic activity of lipases in organic media

Valivety

Halling

Peilow

et al. 1994

European Journal of Biochemistry

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The rates of synthesis of dodecyl decanoate in hexane have been measured as a function of water activity (a,), for various immobilised preparations of the lipases from Rhizomucor miehei and Candida rugosa. Only very large changes in the amount of enzyme adsorbed to the support affect the shape of the ratela, profile; at the highest loadings the profiles tend to become somewhat flatter. A similar levelling can be obtained by pre-adsorbing an inert protein. The effect is probably due to adjacent protein molecules effectively replacing water ; it does not simply reflect mass transfer or interfacial area limitation. The activityla, profile was essentially the same with most supports tested : polypropylene, anion-exchange resin, celite, anion-exchange modified silica. A hydrophobic porous glass support reduced the rate somewhat at intermediate a, values with both enzymes; a polyamide material had this effect only with the lipase from Rh. miehei. The shape of the activityla, profile was not affected by large differences in purity of the lipase preparation, but did differ between forms that probably differ in glycosylation. Overall, relatively few manipulations of the system can significantly affect the shape of the ratela, profiles, which seem to be mainly an intrinsic property of the enzyme molecules used.

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“…If the amount of water required for biocatalysis is expressed as the amount of water bound to the enzyme particles, an optimum in activity is found independent of the solvent used (Zaks and Klibanov, 1988b). An alternative way to explain the difference in the amount of water required in hydrophobic and hydrophilic solvents is that hydrophilic solvents require more water to reach the same water activity (a,) (Valivety et al, 1992a). The water bound by the enzyme particles is likely to be a function of the a, (Halling, 1990) and as a consequence the a, is likely to be a good predictor of the reaction rate.…”

Section: Low Water Activitymentioning

confidence: 99%

Biocatalysis in non-conventional media: Medium engineering aspects (Technical Report)

Vermuë¹,

Tramper²

1995

Pure and Applied Chemistry

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Reaction rate with suspended lipase catalyst shows similar dependence on water activity in different organic solvents

Cited by 276 publications

References 10 publications

Enzymatic Synthesis of a Capsinoid by the Acylation of Vanillyl Alcohol with Fatty Acid Derivatives Catalyzed by Lipases

Enzymatic Synthesis of a Capsinoid by the Acylation of Vanillyl Alcohol with Fatty Acid Derivatives Catalyzed by Lipases

Relationship between water activity and catalytic activity of lipases in organic media

Biocatalysis in non-conventional media: Medium engineering aspects (Technical Report)

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