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Digitale Medien

Improved activity of a lipase by vacuum drying on to a hydrophobic microporous support (1994)

Huang, Fang-Cheng ; Ju, Yi-Hsu

Springer

Biotechnology techniques 8 (1994), S. 827-830

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Details

ISSN: 1573-6784

Quelle: Springer Online Journal Archives 1860-2000

Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: Summary Lipase from Rhizopus arrhizus was immobilized by physical adsorption on hydrophobic microporous polypropylene supports. The immobilized enzyme catalyst was employed for the hydrolysis of palm kernel olein in the presence of n-hexane. The initial rate of lipolysis for vacuum dried immobilized lipase is nearly double that of air dried. The initial rate of lipolysis declines with increase of drying time. Immobilized lipase clearly reveals a relatively high initial rate after 30 days of storage at 4 °C. Stability of the immobilized lipase in buffer could be enhanced up to three-fold that of the free lipase.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00152892

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