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Enzyme-catalyzed processes in organic solvents.

A Zaks, A M Klibanov

    Proceedings of the National Academy of Sciences of the United States of America
    |May 1, 1985
    PubMed
    Summary

    Lipases from porcine pancreas, yeast, and mold efficiently catalyze reactions in organic solvents. Enzyme activity in non-aqueous media depends on the pH used during enzyme recovery, maintaining high catalytic power.

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    Area of Science:

    • Biocatalysis
    • Enzyme kinetics
    • Organic chemistry

    Background:

    • Lipases are versatile enzymes capable of catalyzing various reactions.
    • Enzyme activity in organic solvents is a key area of research for biocatalysis.
    • Understanding enzyme behavior in non-aqueous media is crucial for synthetic applications.

    Purpose of the Study:

    • To investigate the catalytic activity of different lipases in organic solvents.
    • To determine the kinetic behavior of porcine pancreatic lipase in transesterification reactions.
    • To explore the influence of pH on enzyme recovery and subsequent activity in organic media.

    Main Methods:

    • Utilized three types of lipases: porcine pancreatic, yeast, and mold.
    • Performed transesterification reactions in nearly anhydrous organic solvents (e.g., hexane).
    • Analyzed reaction kinetics using Michaelis-Menten models and assessed enzyme activity dependence on pre-treatment pH.

    Main Results:

    • All three lipases demonstrated vigorous catalytic activity in organic solvents.
    • Porcine pancreatic lipase-catalyzed transesterification followed Michaelis-Menten kinetics.
    • Enzyme activity in organic media showed a bell-shaped dependence on the recovery pH, with optimal activity at the enzyme's native pH optimum.
    • Catalytic efficiency in organic solvents was comparable to that in aqueous solutions.
    • Lipases catalyzed esterification, aminolysis, acyl exchange, thiotransesterification, and oximolysis in organic media, with some reactions exclusively occurring in non-aqueous environments.

    Conclusions:

    • Lipases are effective biocatalysts in a wide range of organic solvents.
    • Enzyme performance in non-aqueous systems is significantly influenced by the pH of the aqueous solution from which the enzyme is recovered.
    • The versatility of lipases extends beyond transesterification to various other reactions in organic media, opening new synthetic possibilities.

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