Recombinant thermostable enzyme which forms non-reducing sacchar

Details Recombinant thermostable enzyme which forms non-reducing sacchar Recombinant thermostable enzyme which forms non-reducing sacchar

1995-07-21

1999-11-02

Prouty, Rebecca E.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

435200, 435205, 435193, 435 96, 435 97, 435 99, 435101, C12N 926, C12N 910, C12N 934

Patent

active

059768568

ABSTRACT:
Disclosed is a recombinant thermostable enzyme which has a molecular weight of about 69,000-79,000 daltons and a pI of about 5.4-6.4, and forms non-reducing saccharides having a trehalose structure as an end unit from reducing amylaceous saccharides having a degree of glucose polymerization of at least 3. The enzyme has satisfactorily high thermostability, i.e. it is substantially not inactivated even when incubated in an aqueous solution (pH 7.0) at 85.degree. C. for 60 min, and this facilitates the production of such non-reducing saccharides on an industrial scale and in a satisfactorily-high yield.

REFERENCES:
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patent: 5723327 (1998-03-01), Ikegami et al.
Lama, Licia et al., "Thermostable amylolytic activity from Sulfolobus solfataricus." Biotech Forum Europe, vol. 8, No. 4, pp. 201-203 (1991).
Lama, Licia et al., "Starch conversion with immobilized thermophilic archeabacterium Sulfolobus solfatarious.", Biotechnology Letters, vol. 12, No. 6, pp. 431-432 (Jun. 1990).
Sambrook et al., Molecular Cloning: A Laboratory Manual; Cold Spring Harbour Labratory Press; pp. v-xxxii; 1989.
Southern, E.M.; "Detection of Specific Sequences Among DNA Fragments Separated by Gel Electrophoresis."; Journal of Molecular Biology; vol. 98; pp. 503-571; 1975.
The Amylase Research Society of Japan, editors; Handbook of Amylases and Related Enzymes: Their Sources, Isolation Methods, Properties and Applications. Permagon Press; pp. xi-81; 1988.

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