Thermally stable and positionally non-specific lipase isolated f

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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435921, 435134, C12P 764, C12N 920, C12N 100

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active

052738981

ABSTRACT:
Thermally stable, positionally non-specific lipases native to Candida species of C. antartica, C. tsukubaensis, C. auriculariae, C. humicola, and C. foliarum, are isolated. The lipase of C. antarctica, is preferred. Two lipase activities are elaborated by C. antarctica. One lipase fraction being 43 kD in molecular weight, and of an isoelectric point of about 8.0 and has excellent thermostability. The other fraction being 33 kD in molecular weight and of an isoelectric point of about 6.0 and has high retention of residual activity at pH 10.

REFERENCES:
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patent: 4665029 (1987-05-01), Iwai et al.
patent: 4826767 (1989-05-01), Hansen
patent: 4943530 (1990-07-01), Christner et al.

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