Isolation of a Pure Dextranase from Penicillium funiculosum

Author:

Chaiet L.1,Kempf A. J.1,Harman R.1,Kaczka E.1,Weston R.1,Nollstadt K.1,Wolf F. J.1

Affiliation:

1. Merck Sharp and Dohme Research Laboratories, Rahway, New Jersey 07065

Abstract

A dextranase, produced by Penicillium funiculosum , was purified 1,000-fold to yield the enzyme which was demonstrated by gel electrophoresis and electrofocusing to be a homogeneous protein. The purification method included acetone partition, ammonium sulfate fractionation, gel filtration, iron defecation and precipitation, and diethylaminoethyl-cellulose chromatography. The pure enzyme was also obtained by preparative gel electrophoresis. Gel-permeation chromatography indicates a molecular weight of 41,000. An isoelectric p H of 4.6 was established by electrofocusing. A 1-mg amount of the enzyme hydrolyzes a dextran substrate to yield 27,000 isomaltose reducing units in 2 hr.

Publisher

American Society for Microbiology

Subject

General Pharmacology, Toxicology and Pharmaceutics,General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine

Reference12 articles.

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3. Correlation between molecular weight and elution behavior in the gel chromatography of proteins;Determann H.;J. Chromatogr.,1966

4. The effects of a dextranase preparation on plaque and caries in hamsters, a preliminary report;Fitzgerald R. J.;J. Amer. Dent. Ass.,1968

5. Enzymatic removal of artificial plaques;Fitzgerald R. J.;Arch. Oral Biol.,1968

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